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Characterising four Sarconesiopsis magellanica (Diptera: Calliphoridae) larval fat body-derived antimicrobial peptides

BACKGROUND: The inappropriate use of antibiotics has led to the accelerated growth of resistance to antibiotics. The search for new therapeutic strategies (i.e., antimicrobial peptides-AMPs) has thus become a pressing need. OBJECTIVE: Characterising and evaluating Sarconesiopsis magellanica larval f...

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Autores principales: Pérez, Cindy, Díaz-Roa, Andrea, Bernal, Yuly, Arenas, Nelson E, Kalume, Dario Eluan, Côrtes, Luzia Monteiro de Castro, da, Pedro I, Varela, Yahson, Patarroyo, Manuel A, Torres, Orlando, Bello, Felio J
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Instituto Oswaldo Cruz, Ministério da Saúde 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8291954/
https://www.ncbi.nlm.nih.gov/pubmed/34287503
http://dx.doi.org/10.1590/0074-02760200587
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author Pérez, Cindy
Díaz-Roa, Andrea
Bernal, Yuly
Arenas, Nelson E
Kalume, Dario Eluan
Côrtes, Luzia Monteiro de Castro
da, Pedro I
Varela, Yahson
Patarroyo, Manuel A
Torres, Orlando
Bello, Felio J
author_facet Pérez, Cindy
Díaz-Roa, Andrea
Bernal, Yuly
Arenas, Nelson E
Kalume, Dario Eluan
Côrtes, Luzia Monteiro de Castro
da, Pedro I
Varela, Yahson
Patarroyo, Manuel A
Torres, Orlando
Bello, Felio J
author_sort Pérez, Cindy
collection PubMed
description BACKGROUND: The inappropriate use of antibiotics has led to the accelerated growth of resistance to antibiotics. The search for new therapeutic strategies (i.e., antimicrobial peptides-AMPs) has thus become a pressing need. OBJECTIVE: Characterising and evaluating Sarconesiopsis magellanica larval fat body-derived AMPs. METHODS: Fat body extracts were analysed by reversed-phase high-performance liquid chromatography (RP-HPLC); mass spectrometry was used for characterising the primary structure of the AMPs so found. ProtParam (Expasy) was used for analysing the AMPs’ physico-chemical properties. Synthetic AMPs’ antibacterial activity was evaluated. FINDINGS: Four new AMPs were obtained and called sarconesin III, IV, V and VI. Sarconesin III had an α-helix structure and sarconesins IV, V and VI had linear formations. Oligomer prediction highlighted peptide-peptide interactions, suggesting that sarconesins III, V and VI could form self-aggregations when in contact with the microbial membrane. AMPs synthesised from their native molecules’ sequences had potent activity against Gram-positive bacteria and, to a lesser extent, against Gram-negative and drug-resistant bacteria. Sarconesin VI was the most efficient AMP. None of the four synthetic AMPs had a cytotoxic effect. MAIN CONCLUSIONS: S. magellanica larval fat body-derived antimicrobial peptides are an important source of AMPs and could be used in different antimicrobial therapies and overcoming bacterial resistance.
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spelling pubmed-82919542021-08-03 Characterising four Sarconesiopsis magellanica (Diptera: Calliphoridae) larval fat body-derived antimicrobial peptides Pérez, Cindy Díaz-Roa, Andrea Bernal, Yuly Arenas, Nelson E Kalume, Dario Eluan Côrtes, Luzia Monteiro de Castro da, Pedro I Varela, Yahson Patarroyo, Manuel A Torres, Orlando Bello, Felio J Mem Inst Oswaldo Cruz Original Article BACKGROUND: The inappropriate use of antibiotics has led to the accelerated growth of resistance to antibiotics. The search for new therapeutic strategies (i.e., antimicrobial peptides-AMPs) has thus become a pressing need. OBJECTIVE: Characterising and evaluating Sarconesiopsis magellanica larval fat body-derived AMPs. METHODS: Fat body extracts were analysed by reversed-phase high-performance liquid chromatography (RP-HPLC); mass spectrometry was used for characterising the primary structure of the AMPs so found. ProtParam (Expasy) was used for analysing the AMPs’ physico-chemical properties. Synthetic AMPs’ antibacterial activity was evaluated. FINDINGS: Four new AMPs were obtained and called sarconesin III, IV, V and VI. Sarconesin III had an α-helix structure and sarconesins IV, V and VI had linear formations. Oligomer prediction highlighted peptide-peptide interactions, suggesting that sarconesins III, V and VI could form self-aggregations when in contact with the microbial membrane. AMPs synthesised from their native molecules’ sequences had potent activity against Gram-positive bacteria and, to a lesser extent, against Gram-negative and drug-resistant bacteria. Sarconesin VI was the most efficient AMP. None of the four synthetic AMPs had a cytotoxic effect. MAIN CONCLUSIONS: S. magellanica larval fat body-derived antimicrobial peptides are an important source of AMPs and could be used in different antimicrobial therapies and overcoming bacterial resistance. Instituto Oswaldo Cruz, Ministério da Saúde 2021-07-16 /pmc/articles/PMC8291954/ /pubmed/34287503 http://dx.doi.org/10.1590/0074-02760200587 Text en https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License
spellingShingle Original Article
Pérez, Cindy
Díaz-Roa, Andrea
Bernal, Yuly
Arenas, Nelson E
Kalume, Dario Eluan
Côrtes, Luzia Monteiro de Castro
da, Pedro I
Varela, Yahson
Patarroyo, Manuel A
Torres, Orlando
Bello, Felio J
Characterising four Sarconesiopsis magellanica (Diptera: Calliphoridae) larval fat body-derived antimicrobial peptides
title Characterising four Sarconesiopsis magellanica (Diptera: Calliphoridae) larval fat body-derived antimicrobial peptides
title_full Characterising four Sarconesiopsis magellanica (Diptera: Calliphoridae) larval fat body-derived antimicrobial peptides
title_fullStr Characterising four Sarconesiopsis magellanica (Diptera: Calliphoridae) larval fat body-derived antimicrobial peptides
title_full_unstemmed Characterising four Sarconesiopsis magellanica (Diptera: Calliphoridae) larval fat body-derived antimicrobial peptides
title_short Characterising four Sarconesiopsis magellanica (Diptera: Calliphoridae) larval fat body-derived antimicrobial peptides
title_sort characterising four sarconesiopsis magellanica (diptera: calliphoridae) larval fat body-derived antimicrobial peptides
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8291954/
https://www.ncbi.nlm.nih.gov/pubmed/34287503
http://dx.doi.org/10.1590/0074-02760200587
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