Characterization of novel human intragenic antimicrobial peptides, incorporation and release studies from ureasil-polyether hybrid matrix

Intragenic antimicrobial peptides (IAPs) are internal sequences of proteins with physicochemical similarities to Antimicrobial Peptides (AMPs) that, once identified and synthesized as individual entities, present antimicrobial activity. Many mature proteins encoded by the genomes of virtually any or...

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Bibliographic Details
Published in:	Materials Science & Engineering C Vol. 119; p. 111581
Main Authors:	Mariano, G.H., Gomes de Sá, L.G., Carmo da Silva, E.M., Santos, M.A., Cardozo Fh, J.L., Lira, B.O.V., Barbosa, E.A., Araujo, A.R., Leite, J.R.S.A., Ramada, M.H.S., Bloch Jr, C., Oliveira, A.L., Chaker, J.A., Brand, G.D.
Format:	Journal Article
Language:	English
Published:	Netherlands Elsevier B.V 01-02-2021 Elsevier BV
Subjects:	Anti-Infective Agents - pharmacology Antiinfectives and antibacterials Antimicrobial activity Antimicrobial agents Antimicrobial peptides Antimicrobial polymer Atomic force microscopy Atomic properties Block copolymers Coliforms Controlled release E coli Encrypted peptides Evaluation Genomes Humans Mass spectrometry Mass spectroscopy Materials science Micelles NMR Nuclear magnetic resonance Peptides Phospholipids Polymer films Polymeric films Polymers Pore Forming Cytotoxic Proteins Proteins Proteome data mining Proteomes Sustained release Sustained release device Synthesis Topical application Encrypted peptides Polymeric films Sustained release device Proteome data mining Antimicrobial peptides Antimicrobial polymer
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Summary:	Intragenic antimicrobial peptides (IAPs) are internal sequences of proteins with physicochemical similarities to Antimicrobial Peptides (AMPs) that, once identified and synthesized as individual entities, present antimicrobial activity. Many mature proteins encoded by the genomes of virtually any organism may be regarded as inner reservoirs of IAPs, conferring them ample biotechnological potential. However, IAPs may also share shortcomings with AMPs, such as low half-life in biological media and non-specific adsorption in eukaryotic cells. The present manuscript reports a translational approach that encompasses the uncovering of two novel IAPs from human proteins as well as the first results concerning the incorporation and sustained release of one of these peptides from ureasil-polyether hybrid polymeric films. For such, the software Kamal was used to scan putative IAPs in the human proteome, and two peptides, named Hs05 and Hs06, were identified, synthesized, and tested as antimicrobials. Biophysical assays were conducted using model phospholipid vesicles and 1H NMR solution structures in phospholipid micelles were obtained for the IAP Hs05. This peptide was incorporated in a polymeric matrix composed of the ureasil/PPO-PEO-PPO triblock copolymer, and the resulting films were evaluated by atomic force microscopy and imaging mass spectrometry. The release rate of Hs05 from the polymeric matrix was assessed and the antimicrobial activity of Hs05-loaded hybrid polymeric films was evaluated against the bacterium Escherichia coli. This study represents the first steps towards the development of polymeric films enriched with IAPs obtained from the human proteome as sustained release devices for topical application. [Display omitted] •Fragments of human proteins with antimicrobial activity were identified in silico.•Two of these were synthesized and characterized in biological and biophysical assays.•Peptide Hs05 was incorporated in hybrid ureasil/PPO-PEO-PPO triblock copolymer.•Hs05-hybrid films were evaluated both morphologically and functionally.•A method to obtain antimicrobial peptide-enriched films from proteins is presented.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0928-4931 1873-0191
DOI:	10.1016/j.msec.2020.111581