Switching the N-Capping Region from all-L to all-D Amino Acids in a VEGF Mimetic Helical Peptide

Lucia De Rosa; Donatella Diana; Domenica Capasso; Rachele Stefania; Rossella Di Stasi; Roberto Fattorusso; Luca Domenico D’Andrea

doi:10.3390/molecules27206982

Switching the N-Capping Region from all-L to all-D Amino Acids in a VEGF Mimetic Helical Peptide

Lucia De Rosa, Donatella Diana, Domenica Capasso, Rachele Stefania, Rossella Di Stasi, Roberto Fattorusso, Luca Domenico D’Andrea

Dipartimento di Scienze e Innovazione Tecnologica

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

Abstract

The N-capping region of an α-helix is a short N-terminal amino acid stretch that contributes to nucleate and stabilize the helical structure. In the VEGF mimetic helical peptide QK, the N-capping region was previously demonstrated to be a key factor of QK helical folding. In this paper, we explored the effect of the chiral inversion of the N-capping sequence on QK folding, performing conformational analysis in solution by circular dichroism and NMR spectroscopy. The effect of such a modification on QK stability in serum and the proliferative effect were also evaluated.

Lingua originale	Inglese
Numero di articolo	6982
Rivista	Molecules
Volume	27
Numero di pubblicazione	20
DOI	https://doi.org/10.3390/molecules27206982
Stato di pubblicazione	Pubblicato - ott 2022

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title = "Switching the N-Capping Region from all-L to all-D Amino Acids in a VEGF Mimetic Helical Peptide",

abstract = "The N-capping region of an α-helix is a short N-terminal amino acid stretch that contributes to nucleate and stabilize the helical structure. In the VEGF mimetic helical peptide QK, the N-capping region was previously demonstrated to be a key factor of QK helical folding. In this paper, we explored the effect of the chiral inversion of the N-capping sequence on QK folding, performing conformational analysis in solution by circular dichroism and NMR spectroscopy. The effect of such a modification on QK stability in serum and the proliferative effect were also evaluated.",

keywords = "D-amino acid, N-capping, NMR, peptide conformation, peptide folding, α-helix",

author = "\{De Rosa\}, Lucia and Donatella Diana and Domenica Capasso and Rachele Stefania and \{Di Stasi\}, Rossella and Roberto Fattorusso and D{\textquoteright}Andrea, \{Luca Domenico\}",

note = "Publisher Copyright: {\textcopyright} 2022 by the authors.",

year = "2022",

month = oct,

doi = "10.3390/molecules27206982",

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volume = "27",

journal = "Molecules",

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T1 - Switching the N-Capping Region from all-L to all-D Amino Acids in a VEGF Mimetic Helical Peptide

AU - De Rosa, Lucia

AU - Diana, Donatella

AU - Capasso, Domenica

AU - Stefania, Rachele

AU - Di Stasi, Rossella

AU - Fattorusso, Roberto

AU - D’Andrea, Luca Domenico

PY - 2022/10

Y1 - 2022/10

N2 - The N-capping region of an α-helix is a short N-terminal amino acid stretch that contributes to nucleate and stabilize the helical structure. In the VEGF mimetic helical peptide QK, the N-capping region was previously demonstrated to be a key factor of QK helical folding. In this paper, we explored the effect of the chiral inversion of the N-capping sequence on QK folding, performing conformational analysis in solution by circular dichroism and NMR spectroscopy. The effect of such a modification on QK stability in serum and the proliferative effect were also evaluated.

AB - The N-capping region of an α-helix is a short N-terminal amino acid stretch that contributes to nucleate and stabilize the helical structure. In the VEGF mimetic helical peptide QK, the N-capping region was previously demonstrated to be a key factor of QK helical folding. In this paper, we explored the effect of the chiral inversion of the N-capping sequence on QK folding, performing conformational analysis in solution by circular dichroism and NMR spectroscopy. The effect of such a modification on QK stability in serum and the proliferative effect were also evaluated.

KW - D-amino acid

KW - N-capping

KW - NMR

KW - peptide conformation

KW - peptide folding

KW - α-helix

UR - https://www.scopus.com/pages/publications/85140729443

U2 - 10.3390/molecules27206982

DO - 10.3390/molecules27206982

M3 - Article

SN - 1420-3049

VL - 27

JO - Molecules

JF - Molecules

IS - 20

M1 - 6982

ER -

Switching the N-Capping Region from all-L to all-D Amino Acids in a VEGF Mimetic Helical Peptide

Abstract

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