𝔖 Bobbio Scriptorium
✦   LIBER   ✦

The Position of Aib Residues Defines the Antimicrobial Activity of Aib-Containing Peptides.

✍ Scribed by Hiroshi Yamaguchi; Hiroaki Kodama; Satoshi Osada; Masood Jelokhani-Niaraki; Fumio Kato; Michio Kondo

Publisher
John Wiley and Sons
Year
2010
Weight
24 KB
Volume
33
Category
Article
ISSN
0931-7597

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Helix packing of leucine-rich peptides:
Helix packing of leucine-rich peptides: A parallel leucine ladder in the structure of Boc-Aib-Leu-Aib-Aib-Leu-Leu-Leu-Aib-Leu-Aib-OMe
✍ Dr. Isabella L. Karle; Judith L. Flippen-Anderson; M. Sukumar; P. Balaram 📂 Article 📅 1992 🏛 John Wiley and Sons 🌐 English ⚖ 624 KB

## Abstract The packing of peptide helices in crystals of the leucine‐rich decapeptide Boc‐Aib‐Leu‐Aib‐Aib‐Leu‐Leu‐Leu‐Aib‐Leu‐Aib‐OMe provides an example of ladder‐like leucylleucyl interactions between neighboring molecules. The peptide molecule forms a helix with five 5→1 hydrogen bonds and two

Synthesis of Poly-Aib Oligopeptides and
Synthesis of Poly-Aib Oligopeptides and Aib-Containing Peptides via the ‘Azirine/Oxazolone Method’, and Their Crystal Structures
✍ Ingeborg Dannecker-Dörig; Anthony Linden; Heinz Heimgartner 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 German ⚖ 348 KB

The protected poly-Aib oligopeptides Z-(Aib) n -N(Me)Ph with n ¼ 2 -6 were prepared according to the azirine/oxazolone method, i.e., by coupling amino or peptide acids with 2,2,N-trimethyl-N-phenyl-2H-azirin-3-amine (1a) as an Aib synthon (Scheme 2). Following the same concept, the segments Z-(Aib)

Facile transition between 310- and α-hel
Facile transition between 310- and α-helix: Structures of 8-, 9-, and 10-residue peptides containing the -(Leu-Aib-Ala)2-Phe-Aib-fragment
✍ Isabella L. Karle; Judith L. Flippen-Anderson; R. Gurunath; P. Balaram 📂 Article 📅 1994 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 730 KB

## Abstract A structural transition from a 3~10~‐helix to an α‐helix has been characterized at high resolution for an octapeptide segment located in 3 different sequences. Three synthetic peptides, decapeptide (A) Boc‐Aib‐Trp‐(Leu‐Aib‐Ala)~2~‐Phe‐Aib‐OMe, nonapeptide (B) Boc‐Trp‐(Leu‐Aib‐Ala)~2~‐Ph

Conformations of peptides containing a c
Conformations of peptides containing a chiral cyclic α, α-disubstituted α-amino acid within the sequence of Aib residues
✍ Yosuke Demizu; Masakazu Tanaka; Mitsunobu Doi; Masaaki Kurihara; Haruhiro Okuda; 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 231 KB

## Abstract A single chiral cyclic α,α‐disubstituted amino acid, (3__S__,4__S__)‐1‐amino‐(3,4‐dimethoxy)cyclopentanecarboxylic acid [(__S__,__S__)‐Ac~5~c^dOM^], was placed at the __N__‐terminal or __C__‐terminal positions of achiral α‐aminoisobutyric acid (Aib) peptide segments. The IR and ^1^H NMR

Circular dichroism and conformational an
Circular dichroism and conformational analysis of the membrane-modifying peptide -N-t-Boc-(Aib-L-Ala)5-Gly-Ala-Aib-Pro-Ala-Aib-Aib-Glu-(OBzl)-Gln-OMe with respect to alamethicin
✍ R. Oekonomopulos; G. Jung 📂 Article 📅 1980 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 665 KB

## Abstract The conformational analysis of the CD spectrum is reported for the synthetic and membrane‐modifying nonadecapeptide analog of alamethicin __N__‐__t__‐Boc‐(Aib‐L‐Ala)~5~‐Gly‐Ala‐Aib‐Pro‐Ala‐Aib‐Aib‐Glu(OBzl)‐ Gln‐OMe. The CD data are evaluated according to three different methods and are