Design of peptides: Synthesis, crystal structure, molecular conformation, and conformational calculations of N‐Boc‐<scp>L</scp>‐Phe‐Dehydro‐Ala‐OCH<sub>3</sub>

Padmanabhan, Balasundaram; Dey, Subir; Khandelwal, Bandana; Gs, Rao; Tp, Singh

doi:10.1002/bip.360321002

Cited by 35 publications

(11 citation statements)

References 15 publications

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“…However, this somewhat anomolous behavior of the AAla residue will have to be established with more examples, particularly in peptide sequences, longer than those studied so far. 20,56,57 Crystal structure studies on Ac-Pro-AValNHMe represent the only example of AVal-containing model peptide.j9 The peptide adopts a, @bend between the type I and type 111 conforma- …”

Section: Crystal and Molecular Structural Studiesmentioning

confidence: 99%

Conformational characteristics of peptides containing α,β‐dehydroamino acid residues

1996

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The structural preferences of synthetic peptides containing α,β‐dehydroamino acid residues, as determined by theoretical studies, x‐ray diffraction analyses, and spectroscopic studies, are reviewed. The role of ΔZ Phe residues in stabilizing type II β‐turn structures in small peptides and in nucleating helical structure in longer peptides is exemplified by several crystal as well as solution structural studies. From the few studies reported so far it appears that ΔZ Leu influences the peptide backbone, much like the ΔZ Phe residue, whereas ΔAla prefers the extended conformation, suggesting that the nature of β substituents might influence the conformation restriction behavior of the dehydroresidues. Conformational studies on synthetic peptides containing ΔE, ΔZ Abu, and ΔVal have also been described. © 1996 John Wiley & Sons, Inc.

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Section: Crystal and Molecular Structural Studiesmentioning

confidence: 99%

Conformational characteristics of peptides containing α,β‐dehydroamino acid residues

1996

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“…6 -11 A (Z)-␣,␤-dehydroleucine (⌬ Z Leu) residue having a ␤-isopropyl group also induces a ␤-turn conformation. [12][13][14] On the other hand, dehydroalanine (⌬Ala) without a ␤ substituent adopts an extended conformation, [15][16][17] or induces an inverse ␥-turn in the preceding segment. 18,19 Peptides containing (Z)-or (E)-2-amino-2-butenoic acids (⌬ Z Abu or ⌬ E Abu) with a ␤-methyl group tend to take an extended conformation.…”

Section: Introductionmentioning

confidence: 99%

Structural and conformational properties of (Z)-?-(1-naphthyl)- dehydroalanine residue

Inai¹,

Oshikawa²,

Yamashita³

et al. 2000

Biopolymers

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“…347 (9) 68 (14) 0 5 689 (13) 127 (25) C," 414 (10) 73 (22) CC 608 (14) 138 (26) 265 (6) 49 (9) czl C 2 463 (5) 50 (6) 5 (5) 38 (9) c 6 -30 (7) 53 (10) (8) 75 (15) 6467 (11) 1234 (11) 484 (7) 53 (10) 5834 (7) 636 (7) 537b 59 (6) 7040 (7) 1541 (7) 832 (5) 40 (6) 6922 (9) 1204 (8) 1328 (5) 25 (6) 7745 (11) 1468 (10) 1654 (6) 46 (9) 8544 (12) 751 (12) 1606 (7) 63 (10) 9147 (16) 666 (21) 1234 (9) 94 (20) 8692 (15) 139 (21) 1974 (11) 94 (21) 9835 (24) -115 (36) 1226 (13) 150 (35) 9462 (29) -575 (36) 2032 (18) 170 (41) 9923 (28) -657 (25) 1586 (17) 141 (31) 5972 (9) 1549 (8) 1559 …”

Section: Resultsunclassified

Design of peptides: Crystal and molecular structure of a 3₁₀‐helical peptide N‐Boc‐L‐Phe‐dehydro‐Phe‐L‐Val‐L‐Phe‐dehydro‐Phe‐L‐Val‐Och₃

Padmanabhan

Singh

1993

Biopolymers

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Highly specific peptide structures can be designed by inserting dehydro residues into peptide sequences. The peptide N-Boc-L-Phe-dehydro-Phe-L-Val-L-Phe-dehydro-Phe-L-Val- OCH3, synthesized by conventional procedures, crystallizes from methanol-water mixtures at 4 degrees C in the tetragonal space group P4(3) with cell parameters a = b = 13.829 +/- 0.003 A, c = 27.587 +/- 0.008 A, V = 5275.5 +/- 0.2 A3, Z = 4, dm = 1.152 +/- 0.005 g cm-3, dcal = 1.150 +/- 0.005 g cm-3. The overall residual factor R = 0.084 for 2342 reflections, with 2 theta max = 140 degrees using CuK alpha radiation. The backbone torsion angles are theta 1 = -171(1) degrees, omega 0 = 168(1) degrees, phi 1 = 77(2) degrees, psi 1 = 41(2) degrees, omega 1 = 169(1) degrees, phi 2 = -46(2) degrees, psi 2 = -24(2) degrees, omega 2 = 179(1) degrees, phi 3 = -63(2) degrees, psi 3 = 19(2) degrees, omega 3 = 171(1) degrees, phi 4 = -67(2) degrees, psi 4 = -8(1) degrees, omega 4 = 169(1) degrees, phi 5 = -61(1) degrees, psi 5 = -26(1) degrees, omega 5 = 177(1) degrees, phi 6 = -122(1) degrees, psi 6T = 26(2) degrees. The peptide adopts a 3(10)-helical conformation with three intramolecular hydrogen bonds (i + 3-->i) involving carbonyl oxygen atoms of Phe1, dehydro-Phe2, Val3, and the NH groups of Phe4, dehydro-Phe5, and Val6 with distances of 3.01(1), 2.82(1), and 3.09(2) A, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)

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Design of peptides: Synthesis, crystal structure, molecular conformation, and conformational calculations of N‐Boc‐L‐Phe‐Dehydro‐Ala‐OCH₃

Cited by 35 publications

References 15 publications

Conformational characteristics of peptides containing α,β‐dehydroamino acid residues

Conformational characteristics of peptides containing α,β‐dehydroamino acid residues

Structural and conformational properties of (Z)-?-(1-naphthyl)- dehydroalanine residue

Design of peptides: Crystal and molecular structure of a 3₁₀‐helical peptide N‐Boc‐L‐Phe‐dehydro‐Phe‐L‐Val‐L‐Phe‐dehydro‐Phe‐L‐Val‐Och₃

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Design of peptides: Synthesis, crystal structure, molecular conformation, and conformational calculations of N‐Boc‐L‐Phe‐Dehydro‐Ala‐OCH3

Cited by 35 publications

References 15 publications

Conformational characteristics of peptides containing α,β‐dehydroamino acid residues

Conformational characteristics of peptides containing α,β‐dehydroamino acid residues

Structural and conformational properties of (Z)-?-(1-naphthyl)- dehydroalanine residue

Design of peptides: Crystal and molecular structure of a 310‐helical peptide N‐Boc‐L‐Phe‐dehydro‐Phe‐L‐Val‐L‐Phe‐dehydro‐Phe‐L‐Val‐Och3

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Design of peptides: Synthesis, crystal structure, molecular conformation, and conformational calculations of N‐Boc‐L‐Phe‐Dehydro‐Ala‐OCH₃

Design of peptides: Crystal and molecular structure of a 3₁₀‐helical peptide N‐Boc‐L‐Phe‐dehydro‐Phe‐L‐Val‐L‐Phe‐dehydro‐Phe‐L‐Val‐Och₃