MersV1, PubMed, Checkpoint, bibRecord, 001F17

Effect of ring size on conformation and biological activity of cyclic cationic antimicrobial peptides.

Identifieur interne : 001F17 ( PubMed/Checkpoint ); précédent : 001F16; suivant : 001F18

Effect of ring size on conformation and biological activity of cyclic cationic antimicrobial peptides.

Auteurs : Masoud Jelokhani-Niaraki [Canada] ; Leslie H. Kondejewski ; Laura C. Wheaton ; Robert S. Hodges

Source :

Journal of medicinal chemistry [ 1520-4804 ] ; 2009.

RBID : pubmed:19278255

Descripteurs français

English descriptors

KwdEn :
- Anti-Bacterial Agents (chemical synthesis), Anti-Bacterial Agents (chemistry), Anti-Bacterial Agents (pharmacology), Antifungal Agents (chemical synthesis), Antifungal Agents (chemistry), Antifungal Agents (pharmacology), Antimicrobial Cationic Peptides (chemical synthesis), Antimicrobial Cationic Peptides (chemistry), Antimicrobial Cationic Peptides (pharmacology), Fungi (drug effects), Gram-Negative Bacteria (drug effects), Gram-Positive Bacteria (drug effects), Gramicidin (chemistry), Hemolysis (drug effects), Humans, Hydrophobic and Hydrophilic Interactions, Leucine (chemistry), Lysine (chemistry), Microbial Sensitivity Tests, Models, Molecular, Molecular Conformation, Peptides, Cyclic (chemical synthesis), Peptides, Cyclic (chemistry), Peptides, Cyclic (pharmacology), Stereoisomerism, Structure-Activity Relationship, Valine (chemistry).
MESH :
- chemical , chemical synthesis : Anti-Bacterial Agents, Antifungal Agents, Antimicrobial Cationic Peptides, Peptides, Cyclic.
- chemical , chemistry : Anti-Bacterial Agents, Antifungal Agents, Antimicrobial Cationic Peptides, Gramicidin, Leucine, Lysine, Peptides, Cyclic, Valine.
- chemical , pharmacology : Anti-Bacterial Agents, Antifungal Agents, Antimicrobial Cationic Peptides, Peptides, Cyclic.
- drug effects : Fungi, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemolysis.
- Humans, Hydrophobic and Hydrophilic Interactions, Microbial Sensitivity Tests, Models, Molecular, Molecular Conformation, Stereoisomerism, Structure-Activity Relationship.

Abstract

In a series of cyclic peptides based on GS10, an analogue of gramicidin S (GS), the ring size was varied from 10 to 16 amino acids. Alternative addition of basic and hydrophobic amino acids to the original GS10 construct generated a variety of even-numbered rings, i.e., GS10 [cyclo-(VKLdYPVKLdYP)], GS12 [cyclo-(VKLKdYPKVKLdYP)], GS14 [cyclo-(VKLKVdYPLKVKLdYP), and GS16 [cyclo-(VKLKVKdYPKLKVKLdYP)] (d stands for d-enantiomers). The odd-numbered analogues (11-, 13-, and 15-mers) were derived from these four peptides by either addition or deletion of single basic (Lys) or hydrophobic (Leu or Val) amino acids. The resulting peptides, divided into three groups on the basis of peptide ring size (10- to 12-meric, 13- and 14-meric, and 15- and 16-meric), illustrated a diverse spectrum of biological activity correlated to their ring size, degree of beta-structure disruption, charge, hydrophobicity, amphipathicity, and affinity for lipid membranes. Two of these peptides with potent antimicrobial activities and high therapeutic indexes (4.5- to 10-fold compared with GS) are promising candidates for development of broad-spectrum antibiotics.

DOI: 10.1021/jm801648n
PubMed: 19278255

Affiliations:

Canada

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 002025
to stream PubMed, to step Curation: 002025

Links to Exploration step

pubmed:19278255

Le document en format XML

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<front><div type="abstract" xml:lang="en">In a series of cyclic peptides based on GS10, an analogue of gramicidin S (GS), the ring size was varied from 10 to 16 amino acids. Alternative addition of basic and hydrophobic amino acids to the original GS10 construct generated a variety of even-numbered rings, i.e., GS10 [cyclo-(VKLdYPVKLdYP)], GS12 [cyclo-(VKLKdYPKVKLdYP)], GS14 [cyclo-(VKLKVdYPLKVKLdYP), and GS16 [cyclo-(VKLKVKdYPKLKVKLdYP)] (d stands for d-enantiomers). The odd-numbered analogues (11-, 13-, and 15-mers) were derived from these four peptides by either addition or deletion of single basic (Lys) or hydrophobic (Leu or Val) amino acids. The resulting peptides, divided into three groups on the basis of peptide ring size (10- to 12-meric, 13- and 14-meric, and 15- and 16-meric), illustrated a diverse spectrum of biological activity correlated to their ring size, degree of beta-structure disruption, charge, hydrophobicity, amphipathicity, and affinity for lipid membranes. Two of these peptides with potent antimicrobial activities and high therapeutic indexes (4.5- to 10-fold compared with GS) are promising candidates for development of broad-spectrum antibiotics.</div>
</front>
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<Abstract><AbstractText>In a series of cyclic peptides based on GS10, an analogue of gramicidin S (GS), the ring size was varied from 10 to 16 amino acids. Alternative addition of basic and hydrophobic amino acids to the original GS10 construct generated a variety of even-numbered rings, i.e., GS10 [cyclo-(VKLdYPVKLdYP)], GS12 [cyclo-(VKLKdYPKVKLdYP)], GS14 [cyclo-(VKLKVdYPLKVKLdYP), and GS16 [cyclo-(VKLKVKdYPKLKVKLdYP)] (d stands for d-enantiomers). The odd-numbered analogues (11-, 13-, and 15-mers) were derived from these four peptides by either addition or deletion of single basic (Lys) or hydrophobic (Leu or Val) amino acids. The resulting peptides, divided into three groups on the basis of peptide ring size (10- to 12-meric, 13- and 14-meric, and 15- and 16-meric), illustrated a diverse spectrum of biological activity correlated to their ring size, degree of beta-structure disruption, charge, hydrophobicity, amphipathicity, and affinity for lipid membranes. Two of these peptides with potent antimicrobial activities and high therapeutic indexes (4.5- to 10-fold compared with GS) are promising candidates for development of broad-spectrum antibiotics.</AbstractText>
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Effect of ring size on conformation and biological activity of cyclic cationic antimicrobial peptides.

Effect of ring size on conformation and biological activity of cyclic cationic antimicrobial peptides.

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