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Protein and Peptide Letters, Vol. 5, No. 3, 1998

Contents

Helical Structure of Polypeptides from The C-terminal Half of HIV-1 VPR. Pp. 127-134.
Shenggen Yao, Ahmed A. Azad, Ian G. Macreadie and Raymond S. Norton
[Abstract]

Cytocidal Activities of HIV-1 VPR are Shared by Primate Lentivirus VPR and VPX Relatives. Pp. 135-140.
I. G. Macreadie
[Abstract]

Procedure for the Semisyntheses of Peptide Amides Having a Glutamic or Aspartic Acid a-Amide at the C-terminal. Pp. 141-146.
Dennis B. Henriksen, Marc Rolland, Klaus Breddam and Ole Buchardt
[Abstract]

Self Assembling Peptides Exhibiting Antithrombotic Activity. Pp. 147-154.
C. V. Ramesh, R. Jayakumar and R. Puvanakrishnan
[Abstract]

N-Formyl-Tripeptides Substituted at the Methionine Residue by an Aspartic or Glutamic Acid: Effects on Neutrophil Biological Activity. Pp. 155-158.
Susanna Spisani, Maria E. Ferretti, Elena Fabbri, Serena Alvoni and Giorgio Cavicchioni
[Abstract]

Preliminary Screening of a Hexapeptide Combinatorial Library for Glucosyltransferase (GTE-I) Inhibition. Pp. 159-162.
Kumari S. Devulapalle and Gregory Mooser
[Abstract]

Enzymatic Properties of a-Mannosidase from Trichoderma reesei. Pp. 163-170.
Anna A. Kulminskaya, Elena V. Eneyskaya, Ludmila S. Isaeva-Ivanova, Konstantin A. Shabalin, Andrew N. Savel'ev, Leon V. Backinowsky, Polina L Abronina and Kirill N. Neustroev
[Abstract]

Use of 1-b-Naphthalenesulfonyloxybenzotriazole as Coupling Reagent for Peptide Synthesis in the Presence of Fluorinated Alcohols as Cosolvent. Pp. 171-174.
Sanjay K. Khare, Geeta Singh, Kamlesh C. Agarwal and Bijoy Kundu
[Abstract]

Crystallisation Reports

Preliminary Crystallographic Study of Two Crystal Forms of Rubredoxin from Sulfatereducing bacterium. Pp. 175-176.
Yoshiki Higuchi, Shintaro Misaki, Shigera Sugiyama, Yukio Morimoto, Mari Ogata, Tatsuhiko Yagi and Noritake Yasuoka
[Abstract]

Crystallization and Preliminary Diffraction Studies of a Human Fabm with Anti-I Activity. Pp. 177-180.
A. Cauerhoff, I. Polikarpov, I. Mathov, C. Abatangelo, L. Plotkin, F. A. Goldbaum and J. Leoni
[Abstract]

Crystallization and Preliminary X-ray Analysis of SIII-SPIII, A Phospholipase A2 Isolated from the Venom of Bothrops jararacussu. Pp. 181-184.
Walter F. de Azevedo Jr., M.R.M. Fontes, Richard J. Ward, F.R. Lombardi, A.C.O. Cintra, José R. Gigho and Raghuvir K. Arni
[Abstract]

Abstracts

[Back to top] Helical Structure of Polypeptides from The C-terminal Half of HIV-1 VPR. Shenggen Yao, Ahmed A. Azad, Ian G. Macreadie and Raymond S. Norton.
HIV-1 viral protein R (Vpr), is a 96-residue protein with a number of functions, some of which have been localised to distinct domains in the sequence. This paper describes the solution conformation, determined by NMR, of synthetic peptides encompassing a putative transmembrane helical domain of Vpr associated with formation of cation-selective channels in lipid bilayers. Peptides Vpr50-75 (residues 50-75 of Vpr) and Vpr50-82 both formed a-helices, encompassing residues 53-74 and 53-78, respectively. Thus, Vpr can form a helix long enough to traverse a biological membrane. The helix has some similarities to bee venom melittin, which can also form ion channels.

[Back to top] Cytocidal Activities of HIV-1 VPR are Shared by Primate Lentivirus VPR and VPX Relatives. I. G. Macreadie.
The ability of HIV-1 Vpr to kill human cells has been shown to be due to the sequence, HFRIGCRHSRIG, comprising Vpr amino acid residues 71-82. In this study cell killing by Vpr equivalents in other primate lentiviruses has been examined. Five purified synthetic peptides, related to the bioactive region of HIV-1 Vpr and derived from HIV-2 Vpr and Vpx, SIVmac Vpr and Vpx, and SIVagm Vpx, were shown to share similar abilities to penetrate and kill cells.

[Back to top] Procedure for the Semisyntheses of Peptide Amides Having a Glutamic or Aspartic Acid a-Amide at the C-terminal. Dennis B. Henriksen, Marc Rolland, Klaus Breddam and Ole Buchardt.
Various protected aspartic acid a-arnide and glutamic acid a-amide derivatives were synthesized and applied as nucleophiles in transacylation reactions using carboxypeptidase Y. The benzyl, tert-butyl, cyclohexyl and cyclopentyl ester-type protection for the carboxyl groups were examined and deprotection were achieved by conventional methods.

[Back to top] Self Assembling Peptides Exhibiting Antithrombotic Activity. C. V. Ramesh, R. Jayakumar and R. Puvanakrishnan.
Peptides viz. Boc-L-Arg-L-Pro-lauryl ester laurate (I), Boc-L-Arg-L-Pro-L-Pro-lauryl ester laurate (II) and Boc-L-Arg-L-Pro-stearyl ester stearate (III) were tested in vitro for anticoagulant and fibrinolytic activity. Peptide III was also tested for induction of tissue-plasminogen activator release in a rat model, measured ex vivo. Among the peptides tested, III was found to be more potent than I and II The peptides tended to aggregate in aqueous solutions, and in this aggregated state, the peptides could exhibit the biological activities.

[Back to top] N-Formyl-Tripeptides Substituted at the Methionine Residue by an Aspartic or Glutamic Acid: Effects on Neutrophil Biological Activity. Susanna Spisani, Maria E. Ferretti, Elena Fabbri, Serena Alvoni and Giorgio Cavicchioni.
The formyl-peptides for-Glu-Leu-Phe-OMe 1 and for-Asp-Leu-Phe-OMe 2 were synthesized in order to study the influence of a net negative charge, along the side chain of the first residue, on human neutrophil biological responses. The compounds exert a weak chemotactic as well as secretory activity. Moreover, they are neither able to enhance intracellular calcium levels nor to elicit oxygen-dependent mechanisms. We suggest that the receptor pocket does not accept a net negative charge on the side chain of the first residue.

[Back to top] Preliminary Screening of a Hexapeptide Combinatorial Library for Glucosyltransferase (GTE-I) Inhibition. Kumari S. Devulapalle and Gregory Mooser.
Glucosyltransferases from oral bacteria are significant virulence factors in dental caries initiation. An L-aminoacid synthetic peptide combinatorial library was synthesized and screened for its ability to inhibit the glucosyltransferase activity. One inhibitory hexapeptide was identified to determine the dissociation constant.

[Back to top] Enzymatic Properties of a-Mannosidase from Trichoderma reesei. Anna A. Kulminskaya, Elena V. Eneyskaya, Ludmila S. Isaeva-Ivanova, Konstantin A. Shabalin, Andrew N. Savel'ev, Leon V. Backinowsky, Polina L Abronina and Kirill N. Neustroev.
Kinetic parameters of reactions catalyzed by a-mannosidase from Trichoderma reesei were determined using various mannooligosaccharides as substrates. These reactions were found to go with retention of anomeric configuration. Kinetic experiments revealed the existence of a functionally significant SH-group in the active site of the enzyme. A transglycosylating activity toward p-nitrophenyl-a-D-mannopyranoside was found and single product of this reaction was identified as p-nitrophenyl-a-D-mannopyranose.

[Back to top] Use of 1-b-Naphthalenesulfonyloxybenzotriazole as Coupling Reagent for Peptide Synthesis in the Presence of Fluorinated Alcohols as Cosolvent. Sanjay K. Khare, Geeta Singh, Kamlesh C. Agarwal and Bijoy Kundu.
Solution Phase synthesis of peptides in solvents mixed with fluorinated alcohols have been carried out using 1-b-Naphthalenesulfonyloxybenzotriazole (NSBt) as coupling reagent.

[Back to top] Preliminary Crystallographic Study of Two Crystal Forms of Rubredoxin from Sulfatereducing bacterium. Yoshiki Higuchi, Shintaro Misaki, Shigera Sugiyama, Yukio Morimoto, Mari Ogata, Tatsuhiko Yagi and Noritake Yasuoka.
Two crystal forms, Form I and Form II, of rubredoxin from Desulfovibrio vulgaris Miyazaki F have been obtained by microdialysis and vapor-diffusion methods. The Form I crystals are in space group of P3221 with a=b=43.7, c=50.7Å, whereas the Form II in space group of P21 with a=27.3, b=44.9, c=51.2Å, and b=90.6º. Crystals in both crystal forms diffract at least 2.0Å resolution.

[Back to top] Crystallization and Preliminary Diffraction Studies of a Human Fabm with Anti-I Activity. A. Cauerhoff, I. Polikarpov, I. Mathov, C. Abatangelo, L. Plotkin, F. A. Goldbaum and J. Leoni.
A Fabm from a human monoclonal cold agglutinin (KAU) was obtained by tryptic digestion and purified to homogeneity by FPLC. Crystals were grown by hanging drop vapour diffusion technique against mother liquor containing Sodium Hepes pH 7.5, and PEG 8000 as precipitant. Crystals were found to belong to the trigonal space group P3121(P3221) with the cell parameters a=b=114.233 Å, c=172.787 Å. The crystals diffracted at least to 2.8 Å resolution at a synchrotron beamline.

[Back to top] Crystallization and Preliminary X-ray Analysis of SIII-SPIII, A Phospholipase A2 Isolated from the Venom of Bothrops jararacussu. Walter F. de Azevedo Jr., M.R.M. Fontes, Richard J. Ward, F.R. Lombardi, A.C.O. Cintra, José R. Gigho and Raghuvir K. Arni.
Large single crystals have been obtained of  SIII-SPIII, a phospholipase A2 ftom the venom of Bothrops jararacussu. The crystals belong to the orthorhombic system space group C222, and diffract X-rays to a resolution of 1.9 Å. Preliminary analysis reveals the presence of one molecule in the crystallographic asymmetric unit. The crystal structure is currently being determined using molecular replacement techniques.