Biologically active conformation of tuftsin

Nikiforovich, Gregory V.; Liepina, Inta; Sekacis, Ilmars; Liepiņš, Edvards; Katayev, B.S.; Veretennikova, N.I.; Chipens, G. I.

doi:10.1111/j.1399-3011.1984.tb02719.x

Cited by 9 publications

(3 citation statements)

References 11 publications

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“…Examination of the average structures from our simulations reveals ddferences primarily in the conformations of the amino acid side-chains at the Lys and Arg positions. The average conformation that we have observed in the simulation of the trans isomer in salt solution is similar to Nikiforovich's (12,16) structure. The observed potency of one cyclic analog (12), a peptide with a covalent bridge between the Arg carboxyl group and the N& Lys amino group, supports the view that this structure is biologically active.…”

Section: Figuresupporting

confidence: 81%

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Simulations of conformers of tuftsin and a cyclic tuftsin analog

1995

International Journal of Peptide and Protein Research

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The conformational properties of the configurational isomers of tuftsin, a linear tetrapeptide with the sequence Thr‐Lys‐Pro‐Arg, were investigated with six 1 ns molecular dynamics simulations in explicit water and in a 1.0 M NaCl solution. The average conformation of the cis isomer is a type VI β‐turn. Our results indicate that water‐peptide hydrogen bonding, in addition to intramolecular hydrogen bonds, stabilizes the cis conformer. The trans isomer is neither a β‐ nor a γ‐turn. Results are compared with parallel studies on a cyclic analog of tuftsin, cyclo(Thr‐Lys‐Pro‐Arg‐Gly). The addition of salt does not influence the backbone conformation of the peptide. Differences between the structures are confined to the side‐chain orientations of the Lys and Arg residues. © Munksgaard 1995.

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Section: Figuresupporting

confidence: 81%

“…Since its discovery, tuftsin and its analogs have been the subject of several infrared (9), nuclear magnetic resonance (10)(11)(12)(13) and circular dichroism (1 1, 12, 14) measurements as well as some modeling calculations (15)(16)(17). These studies were aimed at determining the conformation of the peptide in solution.…”

mentioning

confidence: 99%

Simulations of conformers of tuftsin and a cyclic tuftsin analog

1995

International Journal of Peptide and Protein Research

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“…Nikiforovich [19] proposed a quasi-cyclic conformation of tuftsin with φ Lys = −125 °, ψ Lys = 120 °, and ψ Pro = −50 °.…”

Section: Introductionmentioning

confidence: 99%

Quantum Density Functional Theory Studies on Additive Hydration of Tuftsin Tetrapeptide

Karthik

Batu

2022

Journal of Nanomaterials

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Density functional B3LYP method has been used to study the molecular properties of the tuftsin tetrapeptide (threonine-lysine-proline-arginine) and its retro form (arginine-proline-lysine-threonine). The influence of single water molecule on the conformations and relative stabilities of solvated tuftsin complexes has been studied by placing the water molecule at the individual amino acid residues of both the tuftsin complexes. The contribution of four water molecules to the system energetics of tuftsin complexes has also been analyzed. The conformational changes occurred in the solvated tuftsin complexes have been explored through their dihedral angles. The tuftsin is found to be sensitive to structural changes, and our results indicate that water-tuftsin hydrogen bonds (H-bonds), in addition to intramolecular H-bonds, stabilize the β-turn structure with H-bonds between threonine and arginine residues of tuftsin. Difference in the stability of the hydrated complexes is confined to the amino acid residues at which the water molecule is attached to tuftsin. The interaction energy calculations have been used to investigate the strength of the intermolecular H-bond interactions. The AIM theory and NBO analysis were employed to survey the H-bonding patterns in hydrated tuftsin complexes. The maximum ellipticity value (0.129) is noted for the Cα-H (Arg)…O (W) interaction in Tuftsin…4W complex which indicates the higher chance of structural deformation under external perturbations. The interactions between oxygen lone pairs in water and C-H antibond orbitals of tuftsin and retro tuftsin complexes exist with E 2 in the range of 4.03-5.7 and 3.59-4.14 kcal/mol, respectively.

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