Proteolipid

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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, [1] which often provide an interface for interacting with biological membranes [2] and act as lipidons that direct proteins to specific zones. [3]

Contents

Proteolipids were discovered serendipitously in 1951 by Jordi Folch Pi and Marjorie Lees while extracting sulfatides from brain lipids. [4]

They are not to be confused with lipoproteins, a kind of spherical assembly made up of many molecules of lipids and some apolipoproteins.

Structure

Depending on the type of fatty acid attached to the protein, a proteolipid can often contain myristoyl, palmitoyl, or prenyl groups. These groups each serve different functions and have different preferences as to which amino acid residue they attach to. The processes are respectively named myristoylation (usually at N-terminal Gly), palmitoylation (to cysteine), and prenylation (also to cysteine). Despite the seemingly specific names, N-myristoylation and S-palmitoylation can also involve some other fatty acids, most commonly in plants and viral proteolipids. [2] [5] The article on lipid-anchored proteins has more information on these canonical classes.

Lipidated peptides are a type of peptide amphiphile that incorporate one or more alkyl/lipid chains, attached to a peptide head group. As with peptide amphiphiles, they self-assemble depending on the hydrophilic/hydrophobic balance, as well interactions between the peptide units, which is dependent on the charge of the amino acid residues. [6] Lipidated peptides combine the structural features of amphiphilic surfactants with the functions of bioactive peptides, and they are known to assemble into a variety of nanostructures. [7] [8]

Function and application

Due to the desirable properties of peptides such as high receptor affinity and bioactivity, and low toxicity, the use of peptides in therapeutics (i. e. as peptide therapeutics) has great potential; shown by a fast growing market with over 100 approved peptide-based drugs. [9] The disadvantages are that peptides have low oral bioavailability and stability. Lipidation as a chemical modification tool in the development of therapeutic agents has proven to be useful in overcoming these issues, with four lipidized peptide drugs currently approved for use in humans, and various others in clinical trials. [10] Two of the approved drugs are long-acting anti-diabetic GLP-1 analogues liraglutide (Victoza®), and insulin detemir (Levemir®). The other two are the antibiotics daptomycin and polymyxin B.

Lipidated peptides also have applications in other areas, such as use in the cosmetic industry. [6] A commercially available lipidated peptide, Matrixyl, is used in anti-wrinkle creams. Matrixyl is a pentapeptide and has the sequence KTTKS, with an attached palmitoyl lipid chain, that is able to stimulate collagen and fibronectin production in fibroblasts. [11] Several studies have shown promising results of palmitoyl-KTTKS, and topical formulations have been found to significantly reduce fine lines and wrinkles, helping to delay the aging process in the skin. [12] The Hamley group have also carried out investigations of palmitoyl-KTTKS, and found it so self-assemble into nano tapes in the pH range 3-7, in addition to stimulating human dermal and corneal fibroblasts in a concentration dependant manner, suggesting that stimulation occurs above the critical aggregation concentration. [13]

There exist some rarer forms of protein acylation that may not have a membrane-related function. They include serine O-octanoylation in ghrelin, serine O-palmitoleoylation in Wnt proteins, and O-palmitoylation in histone H4 with LPCAT1. Hedgehog proteins are double-modified by (N-)palmitate and cholesterol. Some skin ceramides are proteolipids. [2] The amino group on lysine can also be myristoylation via a poorly-understood mechanism. [14]

In bacteria

All bacteria use proteolipids, sometimes confusingly referred to as bacterial lipoproteins, in their cell membrane. A common modification consists of N-acyl- and S‑diacylglycerol attached to an N-terminal cystine residue. Braun's lipoprotein, found in gram-negative bacteria, is a representative of this group. In addition, Mycobacterium O-mycolate proteins destined for the outer membrane. [15] The plant chloroplast is capable of many of the same modifications that bacteria perform to proteolipids. [16] One database for such N-Acyl Diacyl Glycerylated cell wall proteolipids is DOLOP. [17]

Pathogenic spirochetes, including B. burgdorferi and T. pallidum , use their proteolipid adhesins to stick to victim cells. [18] These proteins are also potent antigens, and are in fact the main immunogens of these two species. [19]

Proteolipids include bacterial antibiotics that aren't synthesised in the ribosome. [10] Products of nonribosomal peptide synthase may also involve a peptide structure linked to lipids. These are usually referred to as "lipopeptides". [15] Bacterial "lipoproteins" and "lipopeptides" (LP) are potent inducers of sepsis, second only to lipopolysaccharide (LPS) in its ability to cause an inflammation response. While LPS is detected by the toll-like receptor TLR4, LPs are detected by TLR2. [20]

Bacillus

Many proteolipids are produced by the Bacillus subtilis family, and are composed of a cyclic structure made up of 7-10 amino acids, and a β-hydroxy fatty acid chain of varying length ranging from 13-19 carbon atoms. [21] These can be divided into three families depending on the structure of the cyclic peptide sequence: surfactins, iturins, and fengycins. [22] [23] [24] Lipidated peptides produced by Bacillus strains have many useful bio-activities such as anti-bacterial, anti- viral, anti-fungal, and anti-tumour properties, [21] [22] making them very attractive for use in a wide range of industries.

Surfactins

As the name implies, surfactins are potent biosurfactants (surfactants produced by bacteria, yeast, or fungi), and they have been shown to reduce the surface tension of water from 72 to 27 mN/m at very low concentrations. [25] Furthermore, surfactins are also able to permeabilize lipid membranes, allowing them to have specific antimicrobial and antiviral activities. [22] [26] [27] Since surfactins are biosurfactants, they have diverse functional properties. These include low toxicity, biodegradability and a higher tolerance towards variation of temperature and pH, [22] making them very interesting for use in a wide range of applications.

Iturins

Iturins are pore‐forming lipopeptides with antifungal activity, and this is dependent on the interaction with the cytoplasmic membrane of the target cells. [22] [23] [28] Mycosubtilin is an iturin isoform that can interact with membranes via its sterol alcohol group, to target ergosterol (a compound found in fungi) to give it antifungal properties. [21] [29]

Fengycins

Fengycins are another class of biosurfactant produced by Bacillus subtilis, with antifungal activity against filamentous fungi. [24] [28] [30] There are two classes of Fengycins, Fengycin A and Fengycin B, with the two only differing by one amino acid at position 6 in the peptide sequence, with the former having an alanine residue, and the latter having valine. [31]

Streptomyces

Daptomycin is another naturally occurring lipidated peptide, produced by the Gram positive bacterium Streptomyces roseoporous . The structure of Daptomycin consists of a decanoyl lipid chain attached to a partially cyclised peptide head group. [6] It has very potent antimicrobial properties and is used as an antibiotic to treat life-threatening conditions caused by Gram positive bacteria including MRSA (methicillin-resistant Staphylococcus aureus) and vancomycin resistant Enterococci. [8] [32] [33] As with the Bacillus subtilis lipidated peptides, the permeation of the cell membrane is what gives it its properties, and the mechanism of action with daptomycin is thought to involve the insertion of the decanoyl chain into the bacterial membrane to cause disruption. This then causes a serious depolarization resulting in the inhibition of various synthesis processes including those of DNA, protein and RNA, leading to apoptosis. [34] [35] [36]

See also

Related Research Articles

<span class="mw-page-title-main">Peptide</span> Short chains of 2–50 amino acids

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

Peptidoglycan or murein is a unique large macromolecule, a polysaccharide, consisting of sugars and amino acids that forms a mesh-like layer (sacculus) that surrounds the bacterial cytoplasmic membrane. The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM). Attached to the N-acetylmuramic acid is an oligopeptide chain made of three to five amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer. Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. This repetitive linking results in a dense peptidoglycan layer which is critical for maintaining cell form and withstanding high osmotic pressures, and it is regularly replaced by peptidoglycan production. Peptidoglycan hydrolysis and synthesis are two processes that must occur in order for cells to grow and multiply, a technique carried out in three stages: clipping of current material, insertion of new material, and re-crosslinking of existing material to new material.

<span class="mw-page-title-main">Transmembrane protein</span> Protein spanning across a biological membrane

A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents.

<span class="mw-page-title-main">Peripheral membrane protein</span> Membrane proteins that adhere temporarily to membranes with which they are associated

Peripheral membrane proteins, or extrinsic membrane proteins, are membrane proteins that adhere only temporarily to the biological membrane with which they are associated. These proteins attach to integral membrane proteins, or penetrate the peripheral regions of the lipid bilayer. The regulatory protein subunits of many ion channels and transmembrane receptors, for example, may be defined as peripheral membrane proteins. In contrast to integral membrane proteins, peripheral membrane proteins tend to collect in the water-soluble component, or fraction, of all the proteins extracted during a protein purification procedure. Proteins with GPI anchors are an exception to this rule and can have purification properties similar to those of integral membrane proteins.

Lantibiotics are a class of polycyclic peptide antibiotics that contain the characteristic thioether amino acids lanthionine or methyllanthionine, as well as the unsaturated amino acids dehydroalanine, and 2-aminoisobutyric acid. They belong to ribosomally synthesized and post-translationally modified peptides.

The periplasm is a concentrated gel-like matrix in the space between the inner cytoplasmic membrane and the bacterial outer membrane called the periplasmic space in Gram-negative bacteria. Using cryo-electron microscopy it has been found that a much smaller periplasmic space is also present in Gram-positive bacteria, between cell wall and the plasma membrane. The periplasm may constitute up to 40% of the total cell volume of gram-negative bacteria, but is a much smaller percentage in gram-positive bacteria.

The cell envelope comprises the inner cell membrane and the cell wall of a bacterium. In Gram-negative bacteria an outer membrane is also included. This envelope is not present in the Mollicutes where the cell wall is absent.

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<span class="mw-page-title-main">Gramicidin</span> Mix of ionophoric antibiotics

Gramicidin, also called gramicidin D, is a mix of ionophoric antibiotics, gramicidin A, B and C, which make up about 80%, 5%, and 15% of the mix, respectively. Each has 2 isoforms, so the mix has 6 different types of gramicidin molecules. They can be extracted from Brevibacillus brevis soil bacteria. Gramicidins are linear peptides with 15 amino acids. This is in contrast to unrelated gramicidin S, which is a cyclic peptide.

<span class="mw-page-title-main">Daptomycin</span> Antibiotic

Daptomycin, sold under the brand name Cubicin among others, is a lipopeptide antibiotic used in the treatment of systemic and life-threatening infections caused by Gram-positive organisms.

<span class="mw-page-title-main">Antimicrobial peptides</span> Class of peptides that have antimicrobial activity

Antimicrobial peptides (AMPs), also called host defence peptides (HDPs) are part of the innate immune response found among all classes of life. Fundamental differences exist between prokaryotic and eukaryotic cells that may represent targets for antimicrobial peptides. These peptides are potent, broad spectrum antimicrobials which demonstrate potential as novel therapeutic agents. Antimicrobial peptides have been demonstrated to kill Gram negative and Gram positive bacteria, enveloped viruses, fungi and even transformed or cancerous cells. Unlike the majority of conventional antibiotics it appears that antimicrobial peptides frequently destabilize biological membranes, can form transmembrane channels, and may also have the ability to enhance immunity by functioning as immunomodulators.

<span class="mw-page-title-main">Amphiphile</span> Hydrophilic and lipophilic chemical compound

An amphiphile, or amphipath, is a chemical compound possessing both hydrophilic and lipophilic (fat-loving) properties. Such a compound is called amphiphilic or amphipathic. Amphiphilic compounds include surfactants and detergents. The phospholipid amphiphiles are the major structural component of cell membranes.

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

Tyrocidine is a mixture of cyclic decapeptides produced by the bacteria Brevibacillus brevis found in soil. It can be composed of 4 different amino acid sequences, giving tyrocidine A–D. Tyrocidine is the major constituent of tyrothricin, which also contains gramicidin. Tyrocidine was the first commercially available antibiotic, but has been found to be toxic toward human blood and reproductive cells. The function of tyrocidine within its host B. brevis is thought to be regulation of sporulation.

<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.

Biosurfactant usually refers to surfactants of microbial origin. Most of the biosurfactants produced by microbes are synthesized extracellularly and many microbes are known to produce biosurfactants in large relative quantities. Some are of commercial interest. As a secondary metabolite of microorganisms, biosurfactants can be processed by the cultivation of biosurfactant producing microorganisms in the stationary phase on many sorts of low-priced substrates like biochar, plant oils, carbohydrates, wastes, etc. High-level production of biosurfactants can be controlled by regulation of environmental factors and growth circumstances.

In biology, an autoinducer is a signaling molecule that enables detection and response to changes in the population density of bacterial cells. Synthesized when a bacterium reproduces, autoinducers pass outside the bacterium and into the surrounding medium. They are a key component of the phenomenon of quorum sensing: as the density of quorum-sensing bacterial cells increases, so does the concentration of the autoinducer. A bacterium’s detection of an autoinducer above some minimum threshold triggers altered gene expression.

A lipopeptide is a molecule consisting of a lipid connected to a peptide. They are able to self-assemble into different structures. Many bacteria produce these molecules as a part of their metabolism, especially those of the genus Bacillus, Pseudomonas and Streptomyces. Certain lipopeptides are used as antibiotics. Due to the structural and molecular properties such as the fatty acid chain, it poses the effect of weakening the cell function or destroying the cell. Other lipopeptides are toll-like receptor agonists. Certain lipopeptides can have strong antifungal and hemolytic activities. It has been demonstrated that their activity is generally linked to interactions with the plasma membrane, and sterol components of the plasma membrane could play a major role in this interaction. It is a general trend that adding a lipid group of a certain length to a lipopeptide will increase its bactericidal activity. Lipopeptides with a higher amount of carbon atoms, for example 14 or 16, in its lipid tail will typically have antibacterial activity as well as anti-fungal activity. Therefore, an increase in the alkyl chain can make lipopeptides soluble in water. As well, it opens the cell membrane of the bacteria, so antimicrobial activity can take place.

<span class="mw-page-title-main">Peptide amphiphile</span>

Peptide amphiphiles (PAs) are peptide-based molecules that self-assemble into supramolecular nanostructures including; spherical micelles, twisted ribbons, and high-aspect-ratio nanofibers. A peptide amphiphile typically comprises a hydrophilic peptide sequence attached to a lipid tail, i.e. a hydrophobic alkyl chain with 10 to 16 carbons. Therefore, they can be considered a type of lipopeptide. A special type of PA, is constituted by alternating charged and neutral residues, in a repeated pattern, such as RADA16-I. The PAs were developed in the 1990s and the early 2000s and could be used in various medical areas including: nanocarriers, nanodrugs, and imaging agents. However, perhaps their main potential is in regenerative medicine to culture and deliver cells and growth factors.

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

Mycosubtilin is a natural lipopeptide with antifungal and hemolytic activities and isolated from Bacillus species. It belongs to the iturin lipopeptide family.

Parvulin-like peptidyl-prolyl isomerase (PrsA), also referred to as putative proteinase maturation protein A (PpmA), functions as a molecular chaperone in Gram-positive bacteria, such as B. subtilis, S. aureus, L. monocytogenes and S. pyogenes. PrsA proteins contain a highly conserved parvulin domain that contains peptidyl-prolyl cis-trans isomerase (PPIase) activity capable of catalyzing the bond N-terminal to proline from cis to trans, or vice versa, which is a rate limiting step in protein folding. PrsA homologs also contain a foldase domain suspected to aid in the folding of proteins but, unlike the parvulin domain, is not highly conserved. PrsA proteins are capable of forming multimers in vivo and in vitro and, when dimerized, form a claw-like structure linked by the NC domains. Most Gram-positive bacteria contain only one PrsA-like protein, but some organisms such as L. monocytogenes, B. anthracis and S. pyogenes contain two PrsAs.

References

Creative Commons by-sa small.svg  This article incorporates text by Jessica Hutchinson available under the CC BY-SA 3.0 license.

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