Impact of a Single Point Mutation on the Antimicrobial and Fibrillogenic Properties of Cryptides from Human Apolipoprotein (78 views)
Pharmaceuticals (ISSN: 1424-8247linking, 1424-8247print), 2021 Jun 29; 14(7): N/D-N/D.
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Paper type: Journal Article,
Impact factor: 5.863, 5-year impact factor: 0
Url: Not available.
Keywords: Anti-Biofilm Activity, Bioactive Cryptides, In Vitro Fibrillogenesis, Single Point Mutation,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.
Istituto Nazionale di Biostrutture e Biosistemi (INBB), 00136 Rome, Italy.
IRCCS SDN, Via E. Gianturco 113, 80143 Naples, Italy.
Physical Chemistry I-Biophysical Chemistry, Faculty of Chemistry and Chemical Biology, TU Dortmund University, 44227 Dortmund, Germany.
Department of Biology, University of Naples Federico II, 80126 Naples, Italy.
Istituto di Biostrutture e Bioimmagini, CNR, 80134 Naples, Italy.
Research Centre on Bioactive Peptides (CIRPeB), University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy.
References:
Not available.
Pharmaceuticals (ISSN: 1424-8247linking, 1424-8247print), 2021 Jun 29; 14(7): N/D-N/D.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.863, 5-year impact factor: 0
Url: Not available.
Keywords: Anti-Biofilm Activity, Bioactive Cryptides, In Vitro Fibrillogenesis, Single Point Mutation,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.
Istituto Nazionale di Biostrutture e Biosistemi (INBB), 00136 Rome, Italy.
IRCCS SDN, Via E. Gianturco 113, 80143 Naples, Italy.
Physical Chemistry I-Biophysical Chemistry, Faculty of Chemistry and Chemical Biology, TU Dortmund University, 44227 Dortmund, Germany.
Department of Biology, University of Naples Federico II, 80126 Naples, Italy.
Istituto di Biostrutture e Bioimmagini, CNR, 80134 Naples, Italy.
Research Centre on Bioactive Peptides (CIRPeB), University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy.
References:
Not available.
Impact of a Single Point Mutation on the Antimicrobial and Fibrillogenic Properties of Cryptides from Human Apolipoprotein
Host defense peptides (HDPs) are gaining increasing interest, since they are endowed with multiple activities, are often effective on multidrug resistant bacteria and do not generally lead to the development of resistance phenotypes. Cryptic HDPs have been recently identified in human apolipoprotein B and found to be endowed with a broad-spectrum antimicrobial activity, with anti-biofilm, wound healing and immunomodulatory properties, and with the ability to synergistically act in combination with conventional antibiotics, while being not toxic for eukaryotic cells. Here, a multidisciplinary approach was used, including time killing curves, differential scanning calorimetry, circular dichroism, ThT binding assays, and transmission electron microscopy analyses. The effects of a single point mutation (Pro → Ala in position 7) on the biological properties of ApoB-derived peptide r(P)ApoB(L)(Pro) have been evaluated. Although the two versions of the peptide share similar antimicrobial and anti-biofilm properties, only r(P)ApoB(L)(Ala) peptide was found to exert bactericidal effects. Interestingly, antimicrobial activity of both peptide versions appears to be dependent from their interaction with specific components of bacterial surfaces, such as LPS or LTA, which induce peptides to form β-sheet-rich amyloid-like structures. Altogether, obtained data indicate a correlation between ApoB-derived peptides self-assembling state and their antibacterial activity.
Host defense peptides (HDPs) are gaining increasing interest, since they are endowed with multiple activities, are often effective on multidrug resistant bacteria and do not generally lead to the development of resistance phenotypes. Cryptic HDPs have been recently identified in human apolipoprotein B and found to be endowed with a broad-spectrum antimicrobial activity, with anti-biofilm, wound healing and immunomodulatory properties, and with the ability to synergistically act in combination with conventional antibiotics, while being not toxic for eukaryotic cells. Here, a multidisciplinary approach was used, including time killing curves, differential scanning calorimetry, circular dichroism, ThT binding assays, and transmission electron microscopy analyses. The effects of a single point mutation (Pro → Ala in position 7) on the biological properties of ApoB-derived peptide r(P)ApoB(L)(Pro) have been evaluated. Although the two versions of the peptide share similar antimicrobial and anti-biofilm properties, only r(P)ApoB(L)(Ala) peptide was found to exert bactericidal effects. Interestingly, antimicrobial activity of both peptide versions appears to be dependent from their interaction with specific components of bacterial surfaces, such as LPS or LTA, which induce peptides to form β-sheet-rich amyloid-like structures. Altogether, obtained data indicate a correlation between ApoB-derived peptides self-assembling state and their antibacterial activity.
Impact of a Single Point Mutation on the Antimicrobial and Fibrillogenic Properties of Cryptides from Human Apolipoprotein
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Impact of a Single Point Mutation on the Antimicrobial and Fibrillogenic Properties of Cryptides from Human Apolipoprotein
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Del Giudice R, Arciello A, Itri F, Merlino A, Monti M, Buonanno M, Penco A, Canetti D, Petruk G, Monti SM, Relini A, Pucci P, Piccoli R, Monti DM
* Protein conformational perturbations in hereditary amyloidosis: Differential impact of single point mutations in ApoAI amyloidogenic variants (528 views)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2016; 1860(2): 434-444.
Impact Factor: 5.476
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* Protein conformational perturbations in hereditary amyloidosis: Differential impact of single point mutations in ApoAI amyloidogenic variants (528 views)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2016; 1860(2): 434-444.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
1 Records (1 excluding Abstracts).
Total impact factor: 5.476 (5.476 excluding Abstracts).
Total 5 year impact factor: 5.725 (5.725 excluding Abstracts).
Total impact factor: 5.476 (5.476 excluding Abstracts).
Total 5 year impact factor: 5.725 (5.725 excluding Abstracts).
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