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COMMUNICATION
Journal Name
Am. Chem. Soc., 2001, 123, 8667; c) S. H. Gellman, Curr.
realized, besides the lateral aggregations of β-strands through
intermolecular H-bonding of solvent exposed amide groups,
the crystal structure also provided evidence of vertical β-sheet
stacking through hydrophobic interactions of amino acid side-
chains along with the additional support from β-turn amide NH
H-bonds. Similar to that of β-strand amino acid side chains, the
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-turn amide group is positioned vertical to the plane. Both
lateral and vertical stacking of three-stranded β-sheets are
shown in Fig. 2e and 2f, respectively. The intermolecular H-
bonding between the NH of Gly 6 and the carbonyl of Gly 11,
along with side-chain hydrophobic interactions, facilitates the
vertical stacking of multiple β-hairpins. In comparison, the
aggregation pattern of P3 is different from that of three-
stranded β-sheets (P1 and P2). In the case of P3, the β-turn
amide (NH and CO) is involved in the H-bonding with solvent
water molecules (Fig. S8), while in P1 and P2 the turn amide
NH is directly involved in the intermolecular H-bonding with
another β-sheet molecule. These crystal structures may serve
Pochan and J. P. Schneider, Biomacromolecules, 2009, 10
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as realistic models to understand the
natural systems.
-sheet aggregations in
In conclusion, we have presented the utilization of
naturally occurring unsaturated -amino acids in the design of
multiple -hairpin structures. The insertion of (E)-alkenyl
13 (a) A. G. Cochran, N. J. Skelton and M. A. Starovasnik, Proc.
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double bonds into the peptide backbone leads to the
restriction in the rotational freedom of β-strands. Both
designed P1 and P2 peptide adopted the three-stranded β-
14 A. J. Riemen and M. L. Waters, Biochemistry, 2009, 48, 1525.
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7
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sheet conformations in single crystals with type I'
structural analysis suggested that the -strands in type I'
hairpins are more closely packed compared to the -hairpin
with the type II' -turn. The work presented here may serve as
-turns. The
16 G. Yamin, P. Ruchala and D. B. Teplow, Biochemistry, 2009,
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-
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,
realistic structural models to understand the self-assemblies of
amyloid fibrils as well as to design biomaterials. In addition,
the insertion of double bond conjugated amides into the
19 M. C. Branco, D. J. Pochan, N. J. Wagner and J. P. Schneider,
Biomaterials, 2009, 30, 1339.
peptide backbone may greatly enhance the scope of -haiprins
20 (a) S. M. Mali, A. Bandyopadhyay, S. V. Jadhav, M. Ganesh
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R.M is thankful to CSIR-India for research fellowship. We thank
DST, Govt. of India (EMR )financial support.
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‡ CCDC Numbers of P1 and P2 are 1435239 and 1032408,
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4 | J. Name., 2012, 00, 1-3
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