Handedness control of peptide helices by amino acid side-chain chirality: Ile/aIle peptides (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Handedness control of peptide helices by amino acid side-chain chirality: Ile/aIle peptides (Articolo in rivista) (literal)

Anno

• 2006-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1002/bip.20534 (literal)

Alternative label

• Andreetto E., Peggion C., Crisma M., Toniolo C. (2006)
  Handedness control of peptide helices by amino acid side-chain chirality: Ile/aIle peptides
  in Biopolymers (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Andreetto E., Peggion C., Crisma M., Toniolo C. (literal)

Pagina inizio

• 490 (literal)

Pagina fine

• 501 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni

• Citazioni WOS: 10 Impact Factor 2006: 2.480 Coautore (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 84 (literal)

Rivista

• Biopolymers (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Institute of Biomolecular Chemistry, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy (literal)

Titolo

• Handedness control of peptide helices by amino acid side-chain chirality: Ile/aIle peptides (literal)

Abstract

• A set of four hexapeptide sequences, each characterized by four strongly helicogenic Aib residues and all combinations of two isomeric Ile/alle residues at positions 2 and 5, was synthesized by solution methods and fully characterized. A detailed solution (by FT-IR absorption, NMR, and CD techniques) and solid/crystalline state (by X-ray diffraction) conformational investigation allowed us to validate our assumption that all four peptides are folded in well-developed 3(10)-helical structures. However, the most relevant conformational conclusion extracted from the present 3D-analysis is that the handedness of the 310-helical structures formed does not seem to be sensitive to the configurational change at the beta-carbon atom of the constituent Ile versus the diastereomeric alle residues (in other words, the dominant control on this important structural parameter appears to be exerted by the chirality of the amino acid alpha-carbon atom). These results complement published-findings on the diverging relative stabilities of the intermolecularly H-bonded beta-sheet structures generated by Ile versus alle homo-oligopeptides. (literal)

Prodotto di

• Istituto di chimica biomolecolare (ICB) (Istituto)
• Peptidi antimicrobici e antivirali (PM.P01.013.001) (Modulo)

Autore CNR

• CLAUDIO TONIOLO (Persona)
• MARCO CRISMA (Unità di personale interno)

Incoming links:

Autore CNR di

• MARCO CRISMA (Unità di personale interno)
• CLAUDIO TONIOLO (Persona)

Prodotto

• Istituto di chimica biomolecolare (ICB) (Istituto)
• Peptidi antimicrobici e antivirali (PM.P01.013.001) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Biopolymers (Rivista)