Intragenic antimicrobial peptides (IAPs) from human proteins with potent antimicrobial and anti-inflammatory activity

PloS One
Guilherme D BrandC Bloch

Abstract

Following the treads of our previous works on the unveiling of bioactive peptides encrypted in plant proteins from diverse species, the present manuscript reports the occurrence of four proof-of-concept intragenic antimicrobial peptides in human proteins, named Hs IAPs. These IAPs were prospected using the software Kamal, synthesized by solid phase chemistry, and had their interactions with model phospholipid vesicles investigated by differential scanning calorimetry and circular dichroism. Their antimicrobial activity against bacteria, yeasts and filamentous fungi was determined, along with their cytotoxicity towards erythrocytes. Our data demonstrates that Hs IAPs are capable to bind model membranes while attaining α-helical structure, and to inhibit the growth of microorganisms at concentrations as low as 1μM. Hs02, a novel sixteen residue long internal peptide (KWAVRIIRKFIKGFIS-NH2) derived from the unconventional myosin 1h protein, was further investigated in its capacity to inhibit lipopolysaccharide-induced release of TNF-α in murine macrophages. Hs02 presented potent anti-inflammatory activity, inhibiting the release of TNF-α in LPS-primed cells at the lowest assayed concentration, 0.1 μM. A three-dimensional solution s...Continue Reading

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Citations

Oct 22, 2020·World Journal of Microbiology & Biotechnology·Hamed MemarianiHamideh Moravvej
Aug 15, 2021·Biochimica Et Biophysica Acta. General Subjects·B P O SantosM T Q de Magalhães

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Methods Mentioned

BETA
protein folding
circular dichroism
flow cytometry
ELISA
NMR
H
peptide resonance

Software Mentioned

MicroCal Origin
CNS
NMRFX Processor
GraphPad
ARIA
FlowJo
GraphPad Prism
Kamal
CCPNMR

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