| Title: |
π‐Turns in Peptides: A Crystal‐State Literature Survey |
| Authors: |
Biondi, Barbara; Formaggio, Fernando; Toniolo, Claudio; Peggion, Cristina; Crisma, Marco |
| Contributors: |
Biondi, Barbara; Formaggio, Fernando; Toniolo, Claudio; Peggion, Cristina; Crisma, Marco |
| Publisher Information: |
John Wiley and Sons Ltd |
| Publication Year: |
2025 |
| Collection: |
Padua Research Archive (IRIS - Università degli Studi di Padova) |
| Subject Terms: |
X‐ray diffraction; linear and cyclic peptide; peptide conformation; statistical analysi; π‐turns |
| Description: |
The results of an analysis on the presence of π-turns, characterized by an i ← i + 5 C=O···H–N intramolecular hydrogen bond, in the X-ray diffraction structures of peptides are discussed. The survey returned a total of 55 π-turn occurrences in linear and cyclic peptides. π-Turns characterized by a helical conformation for residue i + 4, but with a screw sense opposite to that of the three preceding residues, are largely prevailing. They are often found at the C-end of incipient or fully developed α-helices, 310-helices, and mixed α-/310-helices, thus acting as a C-capping motif. However, the structures of two linear peptides and 15 cyclopeptides indicate that these types of π-turns can exist in isolation, without the support of a preceding helix. The frequent presence of additional intramolecular hydrogen bonds internal to the π-turn is also investigated. Cyclopeptides offered examples of two types of π-turns that have no parallel in the structures of proteins. Differently from proteins, π-turns characterized by helical φ, ψ sets of the same screw sense for all internal residues are hitherto unreported in the X-ray diffraction structures of peptides. A suggestion for the rational design in peptides/peptidomimetics of a π-turn featuring the screw-sense reversal of residue i + 4 is proposed. |
| Document Type: |
article in journal/newspaper |
| File Description: |
ELETTRONICO |
| Language: |
English |
| Relation: |
info:eu-repo/semantics/altIdentifier/pmid/40518316; info:eu-repo/semantics/altIdentifier/wos/WOS:001519780300006; volume:31; issue:7; numberofpages:18; journal:JOURNAL OF PEPTIDE SCIENCE; https://hdl.handle.net/11577/3559759 |
| DOI: |
10.1002/psc.70036 |
| Availability: |
https://hdl.handle.net/11577/3559759; https://doi.org/10.1002/psc.70036 |
| Rights: |
info:eu-repo/semantics/openAccess ; license:Creative commons ; license uri:http://creativecommons.org/licenses/by/4.0/ |
| Accession Number: |
edsbas.E7D2B292 |
| Database: |
BASE |