Cecropin A-Melittin B Hybrid CA(1-7)M(2-9) Analogs with Improved Antibacterial Activity, Low Toxicity, and Good Protease Stability

Proceedings of the 37th European Peptide Symposium.

Detalles Bibliográficos
Autores: Talia, Chetty, Mhlongo, Jessica T., Waddad, Ayman Y., Albericio, Fernando, de la Torre, Beatriz G.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2024
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/379746
Acceso en línea:http://hdl.handle.net/10261/379746
Access Level:acceso abierto
Palabra clave:Cetropin A
http://metadata.un.org/sdg/3
Ensure healthy lives and promote well-being for all at all ages
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spelling Cecropin A-Melittin B Hybrid CA(1-7)M(2-9) Analogs with Improved Antibacterial Activity, Low Toxicity, and Good Protease StabilityTalia, ChettyMhlongo, Jessica T.Waddad, Ayman Y.Albericio, Fernandode la Torre, Beatriz G.Cetropin Ahttp://metadata.un.org/sdg/3Ensure healthy lives and promote well-being for all at all agesProceedings of the 37th European Peptide Symposium.Cetropin A and Mellitin peptide hybrids have been a distinguished study for many decades. Cecropin A (1) compromises 37 amino acid and shows good antibacterial activity and is not toxic, however, it is too large to produce at a reasonable cost. Melittin is a 26-residue peptide that shows antibacterial activity, among others, but it is highly toxic to eukaryotic cells (2,3). Previously, it has been established that the hybridization of cecropin A and melittin has the optimal strategy with the combination of residues 1–13 of cecropin A (CA) followed by residues 1–13 of melittin (M), (4) which leads to an antibacterial peptide [CA (1–13)M(1–13)] of broad spectrum with a low hemolytic effect. However, this peptide sequence was still long (26 amino acid residues). Our group has managed to shortened the hybrid sequence even further to 15 amino acid residues, CA(1–7)M(2–9). Managed to synthesize this peptide with its analogs using solid phase peptide synthesis, characterized these peptides using reverse phase High Performance Liquid Chromatograpy (HPLC) and Liqiud Chromatography Mass Spectrometry (LC-MS). According to our findings CA(1–7)M(2–9) and its analogs have good antimicrobial activity, low hemolysis, and have good stability in tryptic digestion. These peptide properties solely depend on the construction of the hybrids, keeping in mind the fragment order, its amino acid composition, length, replacing of certain amino acids and the structure (linear/cyclic).Peer reviewedUniversity of Kwazulu-NatalUniversità di FirenzeConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202520252024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/379746reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3797462026-05-22T06:33:51Z
dc.title.none.fl_str_mv Cecropin A-Melittin B Hybrid CA(1-7)M(2-9) Analogs with Improved Antibacterial Activity, Low Toxicity, and Good Protease Stability
title Cecropin A-Melittin B Hybrid CA(1-7)M(2-9) Analogs with Improved Antibacterial Activity, Low Toxicity, and Good Protease Stability
spellingShingle Cecropin A-Melittin B Hybrid CA(1-7)M(2-9) Analogs with Improved Antibacterial Activity, Low Toxicity, and Good Protease Stability
Talia, Chetty
Cetropin A
http://metadata.un.org/sdg/3
Ensure healthy lives and promote well-being for all at all ages
title_short Cecropin A-Melittin B Hybrid CA(1-7)M(2-9) Analogs with Improved Antibacterial Activity, Low Toxicity, and Good Protease Stability
title_full Cecropin A-Melittin B Hybrid CA(1-7)M(2-9) Analogs with Improved Antibacterial Activity, Low Toxicity, and Good Protease Stability
title_fullStr Cecropin A-Melittin B Hybrid CA(1-7)M(2-9) Analogs with Improved Antibacterial Activity, Low Toxicity, and Good Protease Stability
title_full_unstemmed Cecropin A-Melittin B Hybrid CA(1-7)M(2-9) Analogs with Improved Antibacterial Activity, Low Toxicity, and Good Protease Stability
title_sort Cecropin A-Melittin B Hybrid CA(1-7)M(2-9) Analogs with Improved Antibacterial Activity, Low Toxicity, and Good Protease Stability
dc.creator.none.fl_str_mv Talia, Chetty
Mhlongo, Jessica T.
Waddad, Ayman Y.
Albericio, Fernando
de la Torre, Beatriz G.
author Talia, Chetty
author_facet Talia, Chetty
Mhlongo, Jessica T.
Waddad, Ayman Y.
Albericio, Fernando
de la Torre, Beatriz G.
author_role author
author2 Mhlongo, Jessica T.
Waddad, Ayman Y.
Albericio, Fernando
de la Torre, Beatriz G.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Cetropin A
http://metadata.un.org/sdg/3
Ensure healthy lives and promote well-being for all at all ages
topic Cetropin A
http://metadata.un.org/sdg/3
Ensure healthy lives and promote well-being for all at all ages
description Proceedings of the 37th European Peptide Symposium.
publishDate 2024
dc.date.none.fl_str_mv 2024
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/379746
url http://hdl.handle.net/10261/379746
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv University of Kwazulu-Natal
Università di Firenze
publisher.none.fl_str_mv University of Kwazulu-Natal
Università di Firenze
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
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