Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A

Michele Saviano; Filomena Rossi; Marta Filizola; Carla Isernia; Benedetto Di Blasio; Ettore Benedetti; Carlo Pedone; Ignacy Z. Siemion; Artur Pedyczak

doi:10.1002/bip.360360408

Bioactive peptides: Conformational studies of [TYR⁴] cyclolinopeptide A

Michele Saviano, Filomena Rossi, Marta Filizola, Carla Isernia, Benedetto Di Blasio, Ettore Benedetti, Carlo Pedone, Ignacy Z. Siemion, Artur Pedyczak

Research output: Contribution to journal › Article › peer-review

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Abstract

The solid state conformational analysis of [Tyr⁴] cyclolinopeptide A has been carried out by x‐ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane‐water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P2₁, Z = 2], shows the presence of five intramolecular N‐H OC hydrogen bonds, with formation of one C₁₇ ring structure, one α‐turn (C₁₃), one inverse γ‐turn (C₇), and two β‐turns (C₁₀, one of type III and one of type 1). The Pro¹‐Pro² peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc.

Original language	English
Pages (from-to)	453-460
Number of pages	8
Journal	Biopolymers
Volume	36
Issue number	4
DOIs	https://doi.org/10.1002/bip.360360408
State	Published - Oct 1995
Externally published	Yes

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@article{b62066b8008d4da6a4d741240426f4b8,

title = "Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A",

abstract = "The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x‐ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane‐water mixture [a = 9.849 (5) {\AA}, b = 20.752 (4) {\AA}, c = 16.728 (5) {\AA}, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N‐H OC hydrogen bonds, with formation of one C17 ring structure, one α‐turn (C13), one inverse γ‐turn (C7), and two β‐turns (C10, one of type III and one of type 1). The Pro1‐Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 {\AA}. {\textcopyright} 1995 John Wiley & Sons, Inc.",

author = "Michele Saviano and Filomena Rossi and Marta Filizola and Carla Isernia and {Di Blasio}, Benedetto and Ettore Benedetti and Carlo Pedone and Siemion, {Ignacy Z.} and Artur Pedyczak",

year = "1995",

month = oct,

doi = "10.1002/bip.360360408",

language = "English",

volume = "36",

pages = "453--460",

journal = "Biopolymers",

issn = "0006-3525",

publisher = "John Wiley & Sons Inc.",

number = "4",

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T1 - Bioactive peptides

T2 - Conformational studies of [TYR4] cyclolinopeptide A

AU - Saviano, Michele

AU - Rossi, Filomena

AU - Filizola, Marta

AU - Isernia, Carla

AU - Di Blasio, Benedetto

AU - Benedetti, Ettore

AU - Pedone, Carlo

AU - Siemion, Ignacy Z.

AU - Pedyczak, Artur

PY - 1995/10

Y1 - 1995/10

N2 - The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x‐ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane‐water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N‐H OC hydrogen bonds, with formation of one C17 ring structure, one α‐turn (C13), one inverse γ‐turn (C7), and two β‐turns (C10, one of type III and one of type 1). The Pro1‐Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc.

AB - The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x‐ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane‐water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N‐H OC hydrogen bonds, with formation of one C17 ring structure, one α‐turn (C13), one inverse γ‐turn (C7), and two β‐turns (C10, one of type III and one of type 1). The Pro1‐Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc.

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DO - 10.1002/bip.360360408

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SN - 0006-3525

VL - 36

SP - 453

EP - 460

JO - Biopolymers

JF - Biopolymers

IS - 4

ER -

Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A

Abstract

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Bioactive peptides: Conformational studies of [TYR⁴] cyclolinopeptide A