The Yin and Yang of How N-Terminal Acyl Caps Affect Collagen Triple Helices

FIALA, Tomáš; Rahel HEEB; Luca VIGLIOTTI a Helma WENNEMERS. The Yin and Yang of How N-Terminal Acyl Caps Affect Collagen Triple Helices. Biomacromolecules. Washington: American Chemical Society, 2023, roč. 24, č. 9, s. 3954-3960. ISSN 1525-7797. Dostupné z: https://doi.org/10.1021/acs.biomac.3c00241.

Základní údaje

Originální název

The Yin and Yang of How N-Terminal Acyl Caps Affect Collagen Triple Helices

Autoři

FIALA, Tomáš ORCID; Rahel HEEB; Luca VIGLIOTTI a Helma WENNEMERS

Vydání

Biomacromolecules, Washington, American Chemical Society, 2023, 1525-7797

---

Další údaje

Typ výsledku

Článek v odborném periodiku

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 5.500

Označené pro přenos do RIV

Ne

DOI

https://doi.org/10.1021/acs.biomac.3c00241

Štítky

ne MU, ne RIV

---

Anotace

V originále

N-terminal acylation is a common tool for the installationof functionalmoieties (e.g., sensors or bioactive molecules) on collagen modelpeptides (CMPs). The N-acyl group and its lengthare generally assumed to have little or no influence on the propertiesof the collagen triple helix formed by the CMP. Here, we show thatthe length of short (C-1-C-4) acyl cappinggroups has different effects on the thermal stability of collagentriple helices in POG, OGP, and GPO frames. While the effect of differentcapping groups on the stability of triple helices in the GPO frameis negligible, longer acyl chains stabilize OGP triple helices butdestabilize POG analogues. The observed trends arise from a combinationof steric repulsion, the hydrophobic effect, and n -> pi* interactions. Our study provides a basis for thedesign of N-terminally functionalized CMPs with predictable effectson triple helix stability.