Conformation in solution and dynamics of a structurally constrained linear insect kinin pentapeptide analogue

Moyna, Guillermo; Williams, Howard J.; Nachman, Ronald J.; Scott, A. Ian

doi:10.1002/(sici)1097-0282(19990415)49:5<403::aid-bip6>3.0.co;2-t

Cited by 38 publications

(9 citation statements)

References 35 publications

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“…The sterically hindered α, α‐disubstituted residue Aib replaces the Pro (and/or Ser) at the third position of the pentapeptide core region. Structure sets consistent with ROESY NMR distance constraints obtained by restrained simulated annealing in vacuo indicate a predominant population of a β‐turn involving the Phe 1 ‐Trp 4 region; 31 evidence of a turn in the Phe 2 ‐Gly 5 region was also observed, as was the case with the cyclic kinin analogue. 29…”

Section: Insect Kinins/tyr‐w‐mif‐1supporting

confidence: 57%

“… Superposition of the low‐energy backbone conformers of the cyclic D‐Orn analogue of Tyr‐W‐MIF‐1 (Fig. 6) (gray structure) 8 onto the inactive 2‐5 turn conformation of the insect kinin analogue Phe‐Phe‐Aib‐Trp‐Gly‐NH 2 31 (white structure) demonstrates the similar nature of these two conformations. The 2‐5 turn of the Aib analogue is analogous to the trans Pro 2‐5 turn of the cyclic insect kinin analogue cyclo [Ala‐Phe‐Phe‐Pro‐Trp‐Gly] depicted in Figure 5b.…”

Section: Insect Kinins/tyr‐w‐mif‐1mentioning

confidence: 96%

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Comparison of Active Conformations of the Insectatachykinin/tachykinin and Insect Kinin/Tyr‐W‐MIF‐1 Neuropeptide Family Pairs

Nachman¹,

Moyna²,

Williams³

et al. 1999

Annals of the New York Academy of Sciences

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A comparison of solution conformations of active, restricted-conformation analogues of two sequence-similar insect/vertebrate neuropeptide family pairs shed light on the potential existence of molecular evolutionary relationships. Analogues of the locustatachykinins and the mammalian tachykinin substance P, containing a sterically hindered Aib-NMePhe/Tyr residue block, share similar low-energy turn conformations incorporating a cis peptide bond. Conversely, restricted conformation analogues of the insect kinins and the mammalian opiate peptide Tyr-W-MIF-1, with near identical C-terminal tetrapeptide sequences, adopt different conformations. The insect kinins adopt a cisPro 1-4 beta-turn, in which the Phe1 is critical for bioactivity. Tyr-W-MIF-1 prefers a transPro 2-5 turn, and an additional N-terminal Phe severely inhibits mu-opiate receptor binding. Comparisons of the chemical/conformational requirements for receptor interaction are consistent with a distant evolutionary relationship between the insectatachykinins and tachykinins, but not between the insect kinins and Tyr-W-MIF-1. Therefore, analogues of the insect kinins with pest control potential can be readily designed to avoid mammalian interactions.

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Section: Insect Kinins/tyr‐w‐mif‐1supporting

confidence: 57%

Section: Insect Kinins/tyr‐w‐mif‐1mentioning

confidence: 96%

Comparison of Active Conformations of the Insectatachykinin/tachykinin and Insect Kinin/Tyr‐W‐MIF‐1 Neuropeptide Family Pairs

Nachman¹,

Moyna²,

Williams³

et al. 1999

Annals of the New York Academy of Sciences

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“…In this paper, the Lennard-Jones 12-6 (LJ) potential (eq. 3), which was carried out using AMBER99 force field [27][28][29][30][31], was used to calculate the vdW correction energy term. In eq.…”

Section: Computational Detailsmentioning

confidence: 99%

Evaluation of the individual hydrogen bonding energies in N-methylacetamide chains

Jiang

Wang

2010

Sci. China Chem.

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The individual hydrogen bonding energies in N-methylacetamide chains were evaluated at the MP2/6-31+G** level including BSSE correction and at the B3LYP/6-311++G(3df,2pd) level including BSSE and van der Waals correction. The calculation results indicate that compared with MP2 results, B3LYP calculations without van der Waals correction underestimate the individual hydrogen bonding energies about 5.4 kJ mol 1 for both the terminal and central hydrogen bonds, whereas B3LYP calculations with van der Waals correction produce almost the same individual hydrogen bonding energies as MP2 does for those terminal hydrogen bonds, but still underestimate the individual hydrogen bonding energies about 2.5 kJ mol 1 for the hydrogen bonds near the center. Our calculation results show that the individual hydrogen bonding energy becomes more negative (more attractive) as the chain becomes longer and that the hydrogen bonds close to the interior of the chain are stronger than those near the ends. The weakest individual hydrogen bonding energy is about 29.0 kJ mol 1 found in the dimer, whereas with the growth of the N-methylacetamide chain the individual hydrogen bonding energy was estimated to be as large as 62.5 kJ mol 1 found in the N-methylacetamide decamer, showing that there is a significant hydrogen bond cooperative effect in N-methylacetamide chains. The natural bond orbital analysis indicates that a stronger hydrogen bond corresponds to a larger positive charge for the H atom and a larger negative charge for the O atom in the NH···O=C bond, corresponds to a stronger second-order stabilization energy between the oxygen lone pair and the NH antibonding orbital, and corresponds to more charge transfer between the hydrogen bonded donor and acceptor molecules. N-methylacetamide chain, the individual hydrogen bonding energy, hydrogen bond cooperativity

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“…In Table 3 are the individual hydrogen bonding energies of formamide hexamer, acetamide hexamer, and N ‐methylformamide hexamer obtained from MP2/6‐31+G** with BSSE correction, eq. (1), AMBER99,43–47 CHARMM27,48, 49 and OPLSAA/L50, 51 force fields. As can be seen from MP2, eq.…”

Section: Applicationsmentioning

confidence: 99%

A scheme for rapid prediction of cooperativity in hydrogen bond chains of formamides, acetamides, andN‐methylformamides

Jiang¹,

Sun²,

Wang³

2009

J Comput Chem

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A scheme is proposed in this article to predict the cooperativity in hydrogen bond chains of formamides, acetamides, and N-methylformamides. The parameters needed in the scheme are derived from fitting to the hydrogen bonding energies of MP2/6-31+G** with basis set superposition error (BSSE) correction of the hydrogen bond chains of formamides containing from two to eight monomeric units. The scheme is then used to calculate the individual hydrogen bonding energies in the chains of formamides containing 9 and 12 monomeric units, in the chains of acetamides containing from two to seven monomeric units, in the chains of N-methylformamides containing from two to seven monomeric units. The calculation results show that the cooperativity predicted by the scheme proposed in this paper is in good agreement with those obtained from MP2/6-31+G** calculations by including the BSSE correction, demonstrating that the scheme proposed in this article is reasonable. Based on our scheme, a cooperativity effect of almost 240% of the dimer hydrogen bonding energy in long hydrogen bond formamide chains, a cooperativity effect of almost 190% of the dimer hydrogen bonding energy in long hydrogen bond acetamide chains, and a cooperativity effect of almost 210% of the dimer hydrogen bonding energy in long hydrogen bond N-methylformamide chains are predicted. The scheme is further applied to some heterogeneous chains containing formamide, acetamide, and N-methylformamide. The individual hydrogen bonding energies in these heterogeneous chains predicted by our scheme are also in good agreement with those obtained from Møller-Plesset calculations including BSSE correction.

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Conformation in solution and dynamics of a structurally constrained linear insect kinin pentapeptide analogue

Cited by 38 publications

References 35 publications

Comparison of Active Conformations of the Insectatachykinin/tachykinin and Insect Kinin/Tyr‐W‐MIF‐1 Neuropeptide Family Pairs

Comparison of Active Conformations of the Insectatachykinin/tachykinin and Insect Kinin/Tyr‐W‐MIF‐1 Neuropeptide Family Pairs

Evaluation of the individual hydrogen bonding energies in N-methylacetamide chains

A scheme for rapid prediction of cooperativity in hydrogen bond chains of formamides, acetamides, andN‐methylformamides

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