Peptide

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Drosomycin, an example of a peptide Drosomycin.svg
Drosomycin, an example of a peptide

Peptides are short chains of amino acids linked by peptide bonds. [1] [2] A polypeptide is a longer, continuous, unbranched peptide chain. [3] Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. [4] Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides.

Contents

Peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others.

Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. [5]

Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond. [6] All peptides except cyclic peptides have an N-terminal (amine group) and C-terminal (carboxyl group) residue at the end of the peptide (as shown for the tetrapeptide in the image).

Classification

There are numerous types of peptides that have been classified according to their sources and functions. According to the Handbook of Biologically Active Peptides, some groups of peptides include plant peptides, bacterial/antibiotic peptides, fungal peptides, invertebrate peptides, amphibian/skin peptides, venom peptides, cancer/anticancer peptides, vaccine peptides, immune/inflammatory peptides, brain peptides, endocrine peptides, ingestive peptides, gastrointestinal peptides, cardiovascular peptides, renal peptides, respiratory peptides, opioid peptides, neurotrophic peptides, and blood–brain peptides. [7]

Some ribosomal peptides are subject to proteolysis. These function, typically in higher organisms, as hormones and signaling molecules. Some microbes produce peptides as antibiotics, such as microcins and bacteriocins. [8]

Peptides frequently have post-translational modifications such as phosphorylation, hydroxylation, sulfonation, palmitoylation, glycosylation, and disulfide formation. In general, peptides are linear, although lariat structures have been observed. [9] More exotic manipulations do occur, such as racemization of L-amino acids to D-amino acids in platypus venom. [10]

Nonribosomal peptides are assembled by enzymes, not the ribosome. A common non-ribosomal peptide is glutathione, a component of the antioxidant defenses of most aerobic organisms. [11] Other nonribosomal peptides are most common in unicellular organisms, plants, and fungi and are synthesized by modular enzyme complexes called nonribosomal peptide synthetases. [12]

These complexes are often laid out in a similar fashion, and they can contain many different modules to perform a diverse set of chemical manipulations on the developing product. [13] These peptides are often cyclic and can have highly complex cyclic structures, although linear nonribosomal peptides are also common. Since the system is closely related to the machinery for building fatty acids and polyketides, hybrid compounds are often found. The presence of oxazoles or thiazoles often indicates that the compound was synthesized in this fashion. [14]

Peptones are derived from animal milk or meat digested by proteolysis. [15] In addition to containing small peptides, the resulting material includes fats, metals, salts, vitamins, and many other biological compounds. Peptones are used in nutrient media for growing bacteria and fungi. [16]

Peptide fragments refer to fragments of proteins that are used to identify or quantify the source protein. [17] Often these are the products of enzymatic degradation performed in the laboratory on a controlled sample, but can also be forensic or paleontological samples that have been degraded by natural effects. [18] [19]

Chemical synthesis

Solid-phase peptide synthesis on a rink amide resin using Fmoc-a-amine-protected amino acid Peptide Synthesis.svg
Solid-phase peptide synthesis on a rink amide resin using Fmoc-α-amine-protected amino acid

Protein-peptide interactions

Example of a protein (orange) and peptide (green) interaction. Obtained from Propedia: a peptide-protein interactions database. Protein-peptide interaction.png
Example of a protein (orange) and peptide (green) interaction. Obtained from Propedia: a peptide-protein interactions database.

Peptides can perform interactions with proteins and other macromolecules. They are responsible for numerous important functions in human cells, such as cell signaling, and act as immune modulators. [21] Indeed, studies have reported that 15-40% of all protein-protein interactions in human cells are mediated by peptides. [22] Additionally, it is estimated that at least 10% of the pharmaceutical market is based on peptide products. [21]

Example families

The peptide families in this section are ribosomal peptides, usually with hormonal activity. All of these peptides are synthesized by cells as longer "propeptides" or "proproteins" and truncated prior to exiting the cell. They are released into the bloodstream where they perform their signaling functions.

Antimicrobial peptides

Tachykinin peptides

Vasoactive intestinal peptides

Opioid peptides

Calcitonin peptides

Self-assembling peptides

Other peptides

Terminology

Length

Several terms related to peptides have no strict length definitions, and there is often overlap in their usage:

Number of amino acids

A tripeptide (example Val-Gly-Ala) with green marked amino end (L-valine) and blue marked carboxyl end (L-alanine) Tripeptide Val-Gly-Ala Formula V1.svg
A tripeptide (example Val-Gly-Ala) with
green marked amino end (L-valine) and
blue marked carboxyl end (L-alanine)

Peptides and proteins are often described by the number of amino acids in their chain, e.g. a protein with 158 amino acids may be described as a "158 amino-acid-long protein". Peptides of specific shorter lengths are named using IUPAC numerical multiplier prefixes:

The same words are also used to describe a group of residues in a larger polypeptide (e.g., RGD motif).

Function

See also

Related Research Articles

<span class="mw-page-title-main">Amino acid</span> Organic compounds containing amine and carboxylic groups

Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life.

<span class="mw-page-title-main">Protein</span> Biomolecule consisting of chains of amino acid residues

Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.

<span class="mw-page-title-main">Protein primary structure</span> Linear sequence of amino acids in a peptide or protein

Protein primary structure is the linear sequence of amino acids in a peptide or protein. By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the laboratory. Protein primary structures can be directly sequenced, or inferred from DNA sequences.

<span class="mw-page-title-main">Proteolysis</span> Breakdown of proteins into smaller polypeptides or amino acids

Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion.

<span class="mw-page-title-main">Post-translational modification</span> Chemical changes in proteins following their translation from mRNA

In molecular biology, post-translational modification (PTM) is the covalent process of changing proteins following protein biosynthesis. PTMs may involve enzymes or occur spontaneously. Proteins are created by ribosomes, which translate mRNA into polypeptide chains, which may then change to form the mature protein product. PTMs are important components in cell signalling, as for example when prohormones are converted to hormones.

<span class="mw-page-title-main">Oligopeptide</span> Peptide consisting of two to twenty amino acids

An oligopeptide, is a peptide consisting of two to twenty amino acids, including dipeptides, tripeptides, tetrapeptides, and other polypeptides. Some of the major classes of naturally occurring oligopeptides include aeruginosins, cyanopeptolins, microcystins, microviridins, microginins, anabaenopeptins, and cyclamides. Microcystins are best studied because of their potential toxicity impact in drinking water. A review of some oligopeptides found that the largest class are the cyanopeptolins (40.1%), followed by microcystins (13.4%).

<span class="mw-page-title-main">Proteinogenic amino acid</span> Amino acid that is incorporated biosynthetically into proteins during translation

Proteinogenic amino acids are amino acids that are incorporated biosynthetically into proteins during translation. The word "proteinogenic" means "protein creating". Throughout known life, there are 22 genetically encoded (proteinogenic) amino acids, 20 in the standard genetic code and an additional 2 that can be incorporated by special translation mechanisms.

<span class="mw-page-title-main">Protein structure</span> Three-dimensional arrangement of atoms in an amino acid-chain molecule

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions, such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, cryo-electron microscopy (cryo-EM) and dual polarisation interferometry, to determine the structure of proteins.

Nonribosomal peptides (NRP) are a class of peptide secondary metabolites, usually produced by microorganisms like bacteria and fungi. Nonribosomal peptides are also found in higher organisms, such as nudibranchs, but are thought to be made by bacteria inside these organisms. While there exist a wide range of peptides that are not synthesized by ribosomes, the term nonribosomal peptide typically refers to a very specific set of these as discussed in this article.

<span class="mw-page-title-main">Cyclic peptide</span> Peptide chains which contain a circular sequence of bonds

Cyclic peptides are polypeptide chains which contain a circular sequence of bonds. This can be through a connection between the amino and carboxyl ends of the peptide, for example in cyclosporin; a connection between the amino end and a side chain, for example in bacitracin; the carboxyl end and a side chain, for example in colistin; or two side chains or more complicated arrangements, for example in alpha-amanitin. Many cyclic peptides have been discovered in nature and many others have been synthesized in the laboratory. Their length ranges from just two amino acid residues to hundreds. In nature they are frequently antimicrobial or toxic; in medicine they have various applications, for example as antibiotics and immunosuppressive agents. Thin-Layer Chromatography (TLC) is a convenient method to detect cyclic peptides in crude extract from bio-mass.

A peptide library is a tool for studying proteins. Peptide libraries typically contain a large number of peptides that have a systematic combination of amino acids. Usually, solid phase synthesis, e.g. resin as a flat surface or beads, is used for peptide library generation. Peptide libraries are a popular tool for experiments in drug design, protein–protein interactions, and other biochemical and pharmaceutical applications.

<span class="mw-page-title-main">Surfactin</span> Chemical compound

Surfactin is a cyclic lipopeptide, commonly used as an antibiotic for its capacity as a surfactant. It is an amphiphile capable of withstanding hydrophilic and hydrophobic environments. The Gram-positive bacterial species Bacillus subtilis produces surfactin for its antibiotic effects against competitors. Surfactin showcases antibacterial, antiviral, antifungal, and hemolytic effects.

Peptide signaling plays a significant role in various aspects of plant growth and development and specific receptors for various peptides have been identified as being membrane-localized receptor kinases, the largest family of receptor-like molecules in plants. Signaling peptides include members of the following protein families.

Glycopeptides are peptides that contain carbohydrate moieties (glycans) covalently attached to the side chains of the amino acid residues that constitute the peptide.

Lysine carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction:

<span class="mw-page-title-main">Catgrip</span> Molecular binding feature

Catgrips are small cation-binding molecular features of proteins and peptides. Each consists of the main chain atoms only of three consecutive amino acid residues. The first and third main chain CO groups bind the cations, often calcium, magnesium, potassium or sodium, with no side chain involvement. Many catgrips bind a water molecule instead of a cation; it is hydrogen-bonded to the first and third main chain CO groups. Catgrips are found as calcium-binding features in annexins, matrix metalloproteinases (e.g.serralysins), subtilisins and phospholipase A2. They are also observed in synthetic peptides and in cyclic hexapeptides made from alternating D,L amino acids.

Ribosomally synthesized and post-translationally modified peptides (RiPPs), also known as ribosomal natural products, are a diverse class of natural products of ribosomal origin. Consisting of more than 20 sub-classes, RiPPs are produced by a variety of organisms, including prokaryotes, eukaryotes, and archaea, and they possess a wide range of biological functions.

A proteolipid is a protein covalently linked to lipid molecules, which can be fatty acids, isoprenoids or sterols. The process of such a linkage is known as protein lipidation, and falls into the wider category of acylation and post-translational modification. Proteolipids are abundant in brain tissue, and are also present in many other animal and plant tissues. They include ghrelin, a peptide hormone associated with feeding. Many proteolipids have bound fatty acid chains, which often provide an interface for interacting with biological membranes and act as lipidons that direct proteins to specific zones.

<small>D</small>-Amino acid Class of chemical compounds

D-Amino acids are amino acids where the stereogenic carbon alpha to the amino group has the D-configuration. For most naturally-occurring amino acids, this carbon has the L-configuration. D-Amino acids are occasionally found in nature as residues in proteins. They are formed from ribosomally-derived D-amino acid residues.

<span class="mw-page-title-main">Halovir</span> Group of chemical compounds

Halovir refers to a multi-analogue compound belonging to a group of oligopeptides designated as lipopeptaibols which have membrane-modifying capacity and are fungal in origin. These peptides display interesting microheterogeneity; slight variation in encoding amino acids gives rise to a mixture of closely related analogues and have been shown to have antibacterial/antiviral properties.

References

  1. ↑ Hamley, I. W. (September 2020). introduction to Peptide Science. Wiley. ISBN   978-1-119-69817-3.
  2. ↑ Nelson, David L.; Cox, Michael M. (2005). Principles of Biochemistry (4th ed.). New York: W. H. Freeman. ISBN   0-7167-4339-6.
  3. ↑ Saladin, K. (13 January 2011). Anatomy & physiology: the unity of form and function (6th ed.). McGraw-Hill. p. 67. ISBN   978-0-07-337825-1.
  4. ↑ IUPAC , Compendium of Chemical Terminology , 2nd ed. (the "Gold Book") (1997). Online corrected version: (2006–) " proteins ". doi : 10.1351/goldbook.P04898.
  5. ↑ Ardejani, Maziar S.; Orner, Brendan P. (2013-05-03). "Obey the Peptide Assembly Rules". Science. 340 (6132): 561–562. Bibcode:2013Sci...340..561A. doi:10.1126/science.1237708. ISSN   0036-8075. PMID   23641105. S2CID   206548864.
  6. ↑ IUPAC , Compendium of Chemical Terminology , 2nd ed. (the "Gold Book") (1997). Online corrected version: (2006–) " amino-acid residue in a polypeptide ". doi : 10.1351/goldbook.A00279.
  7. ↑ Abba J. Kastin, ed. (2013). Handbook of Biologically Active Peptides (2nd ed.). Elsevier Science. ISBN   978-0-12-385095-9.
  8. ↑ Duquesne S, Destoumieux-Garzón D, Peduzzi J, Rebuffat S (August 2007). "Microcins, gene-encoded antibacterial peptides from enterobacteria". Natural Product Reports. 24 (4): 708–34. doi:10.1039/b516237h. PMID   17653356.
  9. ↑ Pons M, Feliz M, Antònia Molins M, Giralt E (May 1991). "Conformational analysis of bacitracin A, a naturally occurring lariat". Biopolymers. 31 (6): 605–12. doi:10.1002/bip.360310604. PMID   1932561. S2CID   10924338.
  10. ↑ Torres AM, Menz I, Alewood PF, et al. (July 2002). "D-Amino acid residue in the C-type natriuretic peptide from the venom of the mammal, Ornithorhynchus anatinus, the Australian platypus". FEBS Letters. 524 (1–3): 172–6. doi:10.1016/S0014-5793(02)03050-8. PMID   12135762. S2CID   3015474.
  11. ↑ Meister A, Anderson ME; Anderson (1983). "Glutathione". Annual Review of Biochemistry. 52 (1): 711–60. doi:10.1146/annurev.bi.52.070183.003431. PMID   6137189.
  12. ↑ Hahn M, Stachelhaus T; Stachelhaus (November 2004). "Selective interaction between nonribosomal peptide synthetases is facilitated by short communication-mediating domains". Proceedings of the National Academy of Sciences of the United States of America. 101 (44): 15585–90. Bibcode:2004PNAS..10115585H. doi: 10.1073/pnas.0404932101 . PMC   524835 . PMID   15498872.
  13. ↑ Finking R, Marahiel MA; Marahiel (2004). "Biosynthesis of nonribosomal peptides1". Annual Review of Microbiology. 58 (1): 453–88. doi:10.1146/annurev.micro.58.030603.123615. PMID   15487945.
  14. ↑ Du L, Shen B; Shen (March 2001). "Biosynthesis of hybrid peptide-polyketide natural products". Current Opinion in Drug Discovery & Development. 4 (2): 215–28. PMID   11378961.
  15. ↑ "UsvPeptides- USVPeptides is a leading pharmaceutical company in India". USVPeptides.
  16. ↑ Payne, J. W.; Rose, Anthony H.; Tempest, D. W. (27 September 1974). "Peptides and micro-organisms". Advances in Microbial Physiology, Volume 13. Vol. 13. Oxford, England: Elsevier Science. pp. 55–160. doi:10.1016/S0065-2911(08)60038-7. ISBN   978-0-08-057971-9. OCLC   1049559483. PMID   775944.
  17. ↑ Hummel J, Niemann M, Wienkoop S, Schulze W, Steinhauser D, Selbig J, Walther D, Weckwerth W (2007). "ProMEX: a mass spectral reference database for proteins and protein phosphorylation sites". BMC Bioinformatics. 8 (1): 216. doi: 10.1186/1471-2105-8-216 . PMC   1920535 . PMID   17587460.
  18. ↑ Webster J, Oxley D; Oxley (2005). "Peptide Mass Fingerprinting" . Chemical Genomics. Methods in Molecular Biology. Vol. 310. pp. 227–40. doi:10.1007/978-1-59259-948-6_16. ISBN   978-1-58829-399-2. PMID   16350956.
  19. ↑ Marquet P, Lachâtre G; Lachâtre (October 1999). "Liquid chromatography-mass spectrometry: potential in forensic and clinical toxicology". Journal of Chromatography B. 733 (1–2): 93–118. doi:10.1016/S0378-4347(99)00147-4. PMID   10572976.
  20. ↑ "Propedia v2.3 - Peptide-Protein Interactions Database". bioinfo.dcc.ufmg.br. Retrieved 2023-03-28.
  21. 1 2 Martins, Pedro M.; Santos, Lucianna H.; Mariano, Diego; Queiroz, Felippe C.; Bastos, Luana L.; Gomes, Isabela de S.; Fischer, Pedro H. C.; Rocha, Rafael E. O.; Silveira, Sabrina A.; de Lima, Leonardo H. F.; de Magalhães, Mariana T. Q.; Oliveira, Maria G. A.; de Melo-Minardi, Raquel C. (December 2021). "Propedia: a database for protein–peptide identification based on a hybrid clustering algorithm". BMC Bioinformatics. 22 (1): 1. doi: 10.1186/s12859-020-03881-z . ISSN   1471-2105. PMC   7776311 . PMID   33388027.
  22. ↑ Neduva, Victor; Linding, Rune; Su-Angrand, Isabelle; Stark, Alexander; Masi, Federico de; Gibson, Toby J; Lewis, Joe; Serrano, Luis; Russell, Robert B (2005-11-15). Matthews, Rowena (ed.). "Systematic Discovery of New Recognition Peptides Mediating Protein Interaction Networks". PLOS Biology. 3 (12): e405. doi: 10.1371/journal.pbio.0030405 . ISSN   1545-7885. PMC   1283537 . PMID   16279839.
  23. ↑ Tao, Kai; Makam, Pandeeswar; Aizen, Ruth; Gazit, Ehud (17 Nov 2017). "Self-assembling peptide semiconductors". Science. 358 (6365): eaam9756. doi:10.1126/science.aam9756. PMC   5712217 . PMID   29146781.
  24. ↑ Tao, Kai; Levin, Aviad; Adler-Abramovich, Lihi; Gazit, Ehud (26 Apr 2016). "Fmoc-modified amino acids and short peptides: simple bio-inspired building blocks for the fabrication of functional materials". Chem. Soc. Rev. 45 (14): 3935–3953. doi:10.1039/C5CS00889A. PMID   27115033.
  25. ↑ Tao, Kai; Wang, Jiqian; Zhou, Peng; Wang, Chengdong; Xu, Hai; Zhao, Xiubo; Lu, Jian R. (February 10, 2011). "Self-Assembly of Short Aβ(16−22) Peptides: Effect of Terminal Capping and the Role of Electrostatic Interaction". Langmuir. 27 (6): 2723–2730. doi:10.1021/la1034273. PMID   21309606.
  26. ↑ Ian Hamley (2011). "Self-Assembly of Amphiphilic Peptides" (PDF). Soft Matter. 7 (9): 4122–4138. Bibcode:2011SMat....7.4122H. doi:10.1039/C0SM01218A.
  27. ↑ Kai Tao; Guy Jacoby; Luba Burlaka; Roy Beck; Ehud Gazit (July 26, 2016). "Design of Controllable Bio-Inspired Chiroptic Self-Assemblies". Biomacromolecules. 17 (9): 2937–2945. doi:10.1021/acs.biomac.6b00752. PMID   27461453.
  28. ↑ Kai Tao; Aviad Levin; Guy Jacoby; Roy Beck; Ehud Gazit (23 August 2016). "Entropic Phase Transitions with Stable Twisted Intermediates of Bio‐Inspired Self‐Assembly". Chem. Eur. J. 22 (43): 15237–15241. doi:10.1002/chem.201603882. PMID   27550381.
  29. ↑ Donghui Jia; Kai Tao; Jiqian Wang; Chengdong Wang; Xiubo Zhao; Mohammed Yaseen; Hai Xu; Guohe Que; John R. P. Webster; Jian R. Lu (June 16, 2011). "Dynamic Adsorption and Structure of Interfacial Bilayers Adsorbed from Lipopeptide Surfactants at the Hydrophilic Silicon/Water Interface: Effect of the Headgroup Length". Langmuir. 27 (14): 8798–8809. doi:10.1021/la105129m. PMID   21675796.
  30. ↑ Heitz, Marc; Javor, Sacha; Darbre, Tamis; Reymond, Jean-Louis (2019-08-21). "Stereoselective pH Responsive Peptide Dendrimers for siRNA Transfection". Bioconjugate Chemistry. 30 (8): 2165–2182. doi:10.1021/acs.bioconjchem.9b00403. ISSN   1043-1802. PMID   31398014. S2CID   199519310.
  31. ↑ Boelsma E, Kloek J; Kloek (March 2009). "Lactotripeptides and antihypertensive effects: a critical review". The British Journal of Nutrition. 101 (6): 776–86. doi: 10.1017/S0007114508137722 . PMID   19061526.
  32. ↑ Xu JY, Qin LQ, Wang PY, Li W, Chang C (October 2008). "Effect of milk tripeptides on blood pressure: a meta-analysis of randomized controlled trials". Nutrition. 24 (10): 933–40. doi:10.1016/j.nut.2008.04.004. PMID   18562172.
  33. ↑ Pripp AH (2008). "Effect of peptides derived from food proteins on blood pressure: a meta-analysis of randomized controlled trials". Food & Nutrition Research. 52: 10.3402/fnr.v52i0.1641. doi:10.3402/fnr.v52i0.1641. PMC   2596738 . PMID   19109662.
  34. ↑ Engberink MF, Schouten EG, Kok FJ, van Mierlo LA, Brouwer IA, Geleijnse JM (February 2008). "Lactotripeptides show no effect on human blood pressure: results from a double-blind randomized controlled trial". Hypertension. 51 (2): 399–405. doi: 10.1161/HYPERTENSIONAHA.107.098988 . PMID   18086944.
  35. ↑ Wu, Hongzhong; Ren, Chunyan; Yang, Fang; Qin, Yufeng; Zhang, Yuanxing; Liu, Jianwen (April 2016). "Extraction and identification of collagen-derived peptides with hematopoietic activity from Colla Corii Asini". Journal of Ethnopharmacology. 182: 129–136. doi:10.1016/j.jep.2016.02.019. PMID   26911525.
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