Computational survey of peptides derived from disulphide-bonded protein loops that may serve as mediators of protein-protein interactions

Hdl Handle:
http://hdl.handle.net/10147/333027
Title:
Computational survey of peptides derived from disulphide-bonded protein loops that may serve as mediators of protein-protein interactions
Authors:
Duffy, Fergal J; Devocelle, Marc; Croucher, David R; Shields, Denis C
Citation:
Duffy, F.J. et al., 2014. Computational survey of peptides derived from disulphide-bonded protein loops that may serve as mediators of protein-protein interactions. BMC Bioinformatics. Sep 17, 15(1), 305
Issue Date:
17-Sep-2014
URI:
http://dx.doi.org/10.1186/1471-2105-15-305; http://hdl.handle.net/10147/333027
Abstract:
Abstract Background Bioactive cyclic peptides derived from natural sources are well studied, particularly those derived from non-ribosomal synthetases in fungi or bacteria. Ribosomally synthesised bioactive disulphide-bonded loops represent a large, naturally enriched library of potential bioactive compounds, worthy of systematic investigation. Results We examined the distribution of short cyclic loops on the surface of a large number of proteins, especially membrane or extracellular proteins. Available three-dimensional structures highlighted a number of disulphide-bonded loops responsible for the majority of the likely binding interactions in a variety of protein complexes, due to their location at protein-protein interfaces. We find that disulphide-bonded loops at protein-protein interfaces may, but do not necessarily, show biological activity independent of their parent protein. Examining the conservation of short disulphide bonded loops in proteins, we find a small but significant increase in conservation inside these loops compared to surrounding residues. We identify a subset of these loops that exhibit a high relative conservation, particularly among peptide hormones. Conclusions We conclude that short disulphide-bonded loops are found in a wide variety of biological interactions. They may retain biological activity outside their parent proteins. Such structurally independent peptides may be useful as biologically active templates for the development of novel modulators of protein-protein interactions.
Item Type:
Article
Language:
en
Keywords:
BIOMEDICAL SCIENCE
Local subject classification:
MOLECULAR BIOLOGY; PEPTIDES

Full metadata record

DC FieldValue Language
dc.contributor.authorDuffy, Fergal Jen_GB
dc.contributor.authorDevocelle, Marcen_GB
dc.contributor.authorCroucher, David Ren_GB
dc.contributor.authorShields, Denis Cen_GB
dc.date.accessioned2014-10-21T12:21:10Z-
dc.date.available2014-10-21T12:21:10Z-
dc.date.issued2014-09-17-
dc.identifier.citationDuffy, F.J. et al., 2014. Computational survey of peptides derived from disulphide-bonded protein loops that may serve as mediators of protein-protein interactions. BMC Bioinformatics. Sep 17, 15(1), 305en_GB
dc.identifier.urihttp://dx.doi.org/10.1186/1471-2105-15-305-
dc.identifier.urihttp://hdl.handle.net/10147/333027-
dc.description.abstractAbstract Background Bioactive cyclic peptides derived from natural sources are well studied, particularly those derived from non-ribosomal synthetases in fungi or bacteria. Ribosomally synthesised bioactive disulphide-bonded loops represent a large, naturally enriched library of potential bioactive compounds, worthy of systematic investigation. Results We examined the distribution of short cyclic loops on the surface of a large number of proteins, especially membrane or extracellular proteins. Available three-dimensional structures highlighted a number of disulphide-bonded loops responsible for the majority of the likely binding interactions in a variety of protein complexes, due to their location at protein-protein interfaces. We find that disulphide-bonded loops at protein-protein interfaces may, but do not necessarily, show biological activity independent of their parent protein. Examining the conservation of short disulphide bonded loops in proteins, we find a small but significant increase in conservation inside these loops compared to surrounding residues. We identify a subset of these loops that exhibit a high relative conservation, particularly among peptide hormones. Conclusions We conclude that short disulphide-bonded loops are found in a wide variety of biological interactions. They may retain biological activity outside their parent proteins. Such structurally independent peptides may be useful as biologically active templates for the development of novel modulators of protein-protein interactions.-
dc.language.isoenen
dc.subjectBIOMEDICAL SCIENCEen_GB
dc.subject.otherMOLECULAR BIOLOGYen_GB
dc.subject.otherPEPTIDESen_GB
dc.titleComputational survey of peptides derived from disulphide-bonded protein loops that may serve as mediators of protein-protein interactionsen_GB
dc.typeArticleen
dc.language.rfc3066en-
dc.rights.holderFergal J Duffy et al.; licensee BioMed Central Ltd.-
dc.description.statusPeer Reviewed-
dc.date.updated2014-10-17T23:03:05Z-
All Items in Lenus, The Irish Health Repository are protected by copyright, with all rights reserved, unless otherwise indicated.