Biology:Lipopeptide

From HandWiki
Short description: Compound consisting of a short peptide chain conjugated with an acyl chain
Cyclic lipopeptide antibiotics
Identifiers
SymbolN/A
TCDB1.D.15
OPM superfamily163
OPM protein1t5n

A lipopeptide is a molecule consisting of a lipid connected to a peptide.[1] They are able to self-assemble into different structures.[1][2][3] Many bacteria produce these molecules as a part of their metabolism, especially those of the genus Bacillus, Pseudomonas and Streptomyces.[4] Certain lipopeptides are used as antibiotics.[5][6] 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.[7][8]Other lipopeptides are toll-like receptor agonists.[3] Certain lipopeptides can have strong antifungal and hemolytic activities.[9] It has been demonstrated that their activity is generally linked to interactions with the plasma membrane,[10] and sterol components of the plasma membrane could play a major role in this interaction.[11][12] It is a general trend that adding a lipid group of a certain length (typically C10–C12) to a lipopeptide will increase its bactericidal activity.[13] 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.[13]Therefore, an increase in the alkyl chain can make lipopeptides soluble in water.[14]As well, it opens the cell membrane of the bacteria, so antimicrobial activity can take place.[15]

Lipopeptide detergents (LPDs) are composed of amphiphiles and two alkyl chains which are located on the last part of the peptide backbone. They were designed to mimic the architecture of the native membranes in which two alkyl chains in a lipid molecule facially interact with the hydrophobic segment of MPs.[16]

Examples

See also

References

  1. ↑ 1.0 1.1 "Lipopeptides: from self-assembly to bioactivity". Chemical Communications 51 (41): 8574–83. May 2015. doi:10.1039/c5cc01535a. PMID 25797909. http://centaur.reading.ac.uk/40450/1/c5cc01535a.pdf. 
  2. ↑ "Self-Assembly of the Cyclic Lipopeptide Daptomycin: Spherical Micelle Formation Does Not Depend on the Presence of Calcium Chloride". ChemPhysChem 17 (14): 2118–22. July 2016. doi:10.1002/cphc.201600308. PMID 27043447. http://centaur.reading.ac.uk/66618/3/02.09.2016%20IWH%20DaptomycinAngewChem.pdf. 
  3. ↑ 3.0 3.1 "Toll-like receptor agonist lipopeptides self-assemble into distinct nanostructures". Chemical Communications 50 (100): 15948–51. December 2014. doi:10.1039/c4cc07511k. PMID 25382300. 
  4. ↑ "Microbial lipopeptide production and purification bioprocesses, current progress and future challenges". Biotechnology Journal 12 (7): 1600566. July 2017. doi:10.1002/biot.201600566. PMID 28636078. 
  5. ↑ Hill J, et al., "Lipopeptides as antibacterial agents", US patent granted 6911525, published 28 February 2002, assigned to Cubist Pharmaceuticals Inc
  6. ↑ "Daptomycin: a lipopeptide antibiotic for the treatment of serious Gram-positive infections". The Journal of Antimicrobial Chemotherapy 55 (3): 283–8. March 2005. doi:10.1093/jac/dkh546. PMID 15705644. 
  7. ↑ Czechowicz, Paulina; Nowicka, Joanna (2018-01-01). "Antimicrobial Activity of Lipopeptides" (in en). Advancements of Microbiology 57 (3): 213–227. doi:10.21307/PM-2018.57.3.213. 
  8. ↑ Raaijmakers, Jos M.; De Bruijn, Irene; Nybroe, Ole; Ongena, Marc (November 2010). "Natural functions of lipopeptides from Bacillus and Pseudomonas: more than surfactants and antibiotics". FEMS Microbiology Reviews 34 (6): 1037–1062. doi:10.1111/j.1574-6976.2010.00221.x. ISSN 1574-6976. PMID 20412310. 
  9. ↑ "Iturins, a special class of pore-forming lipopeptides: biological and physicochemical properties". Toxicology 87 (1–3): 151–74. February 1994. doi:10.1016/0300-483X(94)90159-7. PMID 8160184. 
  10. ↑ "Interactions des antibiotiques ituriniques avec la membrane plasmique. Apport des systèmes biomimétiques des membranes (synthèse bibliographique).". Biotechnologie, Agronomie, Société et Environnement. 17 (3): 505–16. September 2013. 
  11. ↑ "Interactions of the antifungal mycosubtilin with ergosterol-containing interfacial monolayers". Biochimica et Biophysica Acta (BBA) - Biomembranes 1818 (5): 1302–8. May 2012. doi:10.1016/j.bbamem.2012.01.020. PMID 22306791. 
  12. ↑ "Specific interactions of mycosubtilin with cholesterol-containing artificial membranes". Langmuir: The ACS Journal of Surfaces and Colloids 27 (17): 10785–92. September 2011. doi:10.1021/la200767e. PMID 21766869. 
  13. ↑ 13.0 13.1 Kanwar, Shamsher S.; Meena, Khem Raj (2015). "Lipopeptides as the Antifungal and Antibacterial Agents: Applications in Food Safety and Therapeutics" (in en). BioMed Research International 2015: 473050. doi:10.1155/2015/473050. PMID 25632392. 
  14. ↑ Czechowicz, Paulina; Nowicka, Joanna (2018-01-01). "Antimicrobial Activity of Lipopeptides" (in en). Advancements of Microbiology 57 (3): 213–227. doi:10.21307/PM-2018.57.3.213. 
  15. ↑ Nasompag, Sawinee; Dechsiri, Punpimon; Hongsing, Nuttaya; Phonimdaeng, Prasart; Daduang, Sakda; Klaynongsruang, Sompong; Camesano, Terri A.; Patramanon, Rina (October 2015). "Effect of acyl chain length on therapeutic activity and mode of action of the CX-KYR-NH2 antimicrobial lipopeptide" (in en). Biochimica et Biophysica Acta (BBA) - Biomembranes 1848 (10): 2351–2364. doi:10.1016/j.bbamem.2015.07.004. PMID 26170198. 
  16. ↑ Zhang, Shuguang; Corin, Karolina (2018). "Peptide surfactants in membrane protein purification and stabilization". in Koutsopoulos, Sotirios. Peptide Applications in Biomedicine, Biotechnology and Bioengineering. Elsevier Science. ISBN 978-0-08-100736-5. 

Further reading





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