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Aggregation studies in crystals of apolar helical peptides: Boc-Aib-Val-Ala-Leu-Aib-Val-Ala-Leu-Aib-OMe

✍ Scribed by KARLE, ISABELLA L. ;FLIPPEN-ANDERSON, JUDITH L. ;UMA, K. ;BALARAM, P.

Book ID: 115098848
Publisher: Wiley (Blackwell Publishing)
Year: 2009
Tongue: English
Weight: 440 KB
Volume: 32
Category: Article
ISSN: 0367-8377
DOI: 10.1111/j.1399-3011.1988.tb01385.x

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## Synopsis A second example of insertion of a water molecule into the helical backbone of an apolar peptide is presented here and compared to a similar occurrence in a longer peptide with the same type of sequence of residues, i.e., Boc-Aib-(Ala-Leu-fib),-OMe. The backbone of the title compound a

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Leu-Ala-Leu-Aib-OMe, have been obtained. Antiparallel helix aggregation is observed in crystals grown from methanol ( A ) , while completely parallel packing is observed in crystals from isopropanol ( B ) or an ethylene glycol-ethanol mixture ( C ) . Crystals B and C are very similar in molecular co

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Effects of End Group and Aggregation on Helix Conformation: Crystal Structure of Ac-(Aib-Val-Ala-Leu)2-Aib- OMe

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## Abstract The role of end groups in determining stereochemistry and packing in hydrophobic helical peptides has been investigated using an α‐aminosobutyric acid (Aib) containing model nonapeptide sequence. In contrast to the Boc‐analogue, Ac‐(Aib‐Val‐Ala‐Leu)~2~‐Aib‐OMe crystallizes with two inde