Protein and Peptide Letters, Vol. 6, No. 6, 1999

Contents

Synthesis of a New Group of Deltorphin I/II Analogs Modified in the Address Domain with g-Amino Acids, and QSAR Study of their d/m Opioid Binding. Pp. 359-366.
Deborah L. Heyl, Medha D. Sanvordekar, Guzin Dogruyol, Mohamed D. Salamoun, David W. Rodgers, Kutralanathan Renganathan, Carol Mousigian and Stephen E. Schullery
[Abstract]

EPO Mimetic Peptide Fused into PAI-1 Augments its EPO Activity. Pp. 367-372.
Kuai Le-tian, Wu Chun-lei, Zhang Jing, Qiu Qi-feng, Zhou Ai-wu, Wang Shi-quan, Zhang He-yun, Song Qian, Liao Shu-ning, Han Yu, Liu Jian-ning and Ma Zhong
[Abstract]

Effect of Copper Ion on Conformations of Short Alanine-Based Peptides with Single TRP/HIS Stacking Interactions. Pp. 373-378.
Jin Zou and Naoki Sugimoto
[Abstract]

Antiallergic Activity of Novel Hexapeptides Related to Immunoglobulin E. Pp. 379-384.
Bijoy Kundu, Manisha Shukla, Sanjay K. Khare, Prem P. Gupta, Rashmi Singh and Amarnath
[Abstract]

a-Amylase Inhibitors from Cowpea Seeds. Pp. 385-390.
Francislete R. Melo, Maurício P. Sales, Lucilene S. Pereira, Carlos Bloch Jr., Octávio L Franco and Maria B. Ary
[Abstract]

Solid-Phase Synthesis of Hydrophobic Peptides on 1,6-Hexanediol Diacrylate Crosslinked Polystyrene Resin: Comparison with Merrifield Resin. Pp. 391-398.
C. Arunan and V.N. Rajasekharan Pillai
[Abstract]

Crystallisation Report

Crystallization and A Preliminary Crystallographic Analysis of the Catalytic Domain of Chitinase Al from Bacillus Circulans WL-12. Pp. 399-402.
Takuo Matsumoto, Takamasa Nonaka, Haruhiko Katouda, Masayuki Hashimoto, Takeshi Watanabe and Yukio Mitsui
[Abstract]

Purification and Crystallization of a Catechol 2,3-Dioxygenase PheB from Bacillus stearothermophilus BR219. Pp. 403-406.
Keisuko Sugimoto, Toshiya Senda, Eiji Masai, Kazuhide Kimbara, Masao Fukuda and Yukio Mitsui
[Abstract]

Crystallization and Preliminary X-ray Crystallographic Studies of Ribonuclease LE from Lycopersicon esculentum. Pp. 407-410.
Nobutada Tanaka, Jun Arai, Norio Inokuchi, Takashi Koyama, Kazuko Ohgi, Masachika Irie and Kazuo T. Nakamura
[Abstract]

Abstracts

[Back to top] Synthesis of a New Group of Deltorphin I/II Analogs Modified in the Address Domain with g-Amino Acids, and QSAR Study of their d/m Opioid Binding. Deborah L. Heyl, Medha D. Sanvordekar, Guzin Dogruyol, Mohamed D. Salamoun, David W. Rodgers, Kutralanathan Renganathan, Carol Mousigian and Stephen E. Schullery.
The d selectivity of the opioid heptapeptides deltorphin I and II has been attributed to the C-terminal "address" domain, the hydrophobic Val⁵-Val⁶ residues apparently playing a topographical role. We now report the synthesis, opioid binding affinities, and a QSAR study of a series of peptides in which these valine residues were replaced with g-amino acids. Results support a conformation stabilization role for this domain, rather than interaction with a receptor binding pocket.

[Back to top] EPO Mimetic Peptide Fused into PAI-1 Augments its EPO Activity. Kuai Le-tian, Wu Chun-lei, Zhang Jing, Qiu Qi-feng, Zhou Ai-wu, Wang Shi-quan, Zhang He-yun, Song Qian, Liao Shu-ning, Han Yu, Liu Jian-ning and Ma Zhong.
EPO Mimetic Peptide (EMP) encoding sequence was inserted into the gene of PAI-1 between P2'-P3', generating a novel gene of PAI-1/EMP (PMP). It was cloned into pETl1d expression vector; and a 43kDa protein was expressed in inclusion bodies with an expression level over 30%. The PMP protein was purified by DEAE ion-exchange chromatography to one band in SDS-PAGE (Silver Stained). The EPO activity of PMP was determined by Reticulocyte Counting Assay to be 5000IU/mg, 2500 folds that of EMP (as reported).

[Back to top] Effect of Copper Ion on Conformations of Short Alanine-Based Peptides with Single TRP/HIS Stacking Interactions. Jin Zou and Naoki Sugimoto.
Cu²⁺ has an apparent promoting effect on deaggregating b-sheet conformation, conformational transitions from b-sheet to a-helix, and enhancing a-helix conformation of short alanine-based peptides with single Trp/His (W/H) stacking interactions in different geometrical spacings and positions, respectively.

[Back to top] Antiallergic Activity of Novel Hexapeptides Related to Immunoglobulin E. Bijoy Kundu, Manisha Shukla, Sanjay K. Khare, Prem P. Gupta, Rashmi Singh and Amarnath.
Eight novel hexapeptides corresponding to IgE Fc region (330-334) have been synthesized and evaluated for antiallergic activity by studying antiPCA as well as mast cell stabilizing activity. One of the peptides (CDRI compound 95/220) exhibited high order of antiallergic activity.

[Back to top] a-Amylase Inhibitors from Cowpea Seeds. Francislete R. Melo, Maurício P. Sales, Lucilene S. Pereira, Carlos Bloch Jr., Octávio L Franco and Maria B. Ary.
This work describes the first isolation and partial characterization of a-amylase inhibitors from cowpea (Vigna unguiculata) seeds. a-Amylase inhibitors were isolated using an affinity chromatography on Red Sepharose CL-6B. The bound Red Sepharose fraction was active against a-amylases from Bacillus sp., Aspergilus oryzae, V unguiculata seeds and also against a-amylases from Callosobruchus maculatus larvae.

[Back to top] Solid-Phase Synthesis of Hydrophobic Peptides on 1,6-Hexanediol Diacrylate Crosslinked Polystyrene Resin: Comparison with Merrifield Resin. C. Arunan and V.N. Rajasekharan Pillai.
A novel polymer support based on 1,6-hexanediol diacrylate and polystyrene was developed. The resin showed better solvation in solvents used for peptide synthesis than Merrifield resin. The synthetic utility of the new support has been illustrated with the synthesis of some hydrophobic peptides which have high affinity for aggregation. The yield and purity of the peptides were high compared to when Merrifield resin was used.

[Back to top] Crystallization and A Preliminary Crystallographic Analysis of the Catalytic Domain of Chitinase Al from Bacillus Circulans WL-12. Takuo Matsumoto, Takamasa Nonaka, Haruhiko Katouda, Masayuki Hashimoto, Takeshi Watanabe and Yukio Mitsui.
The catalytic domain of chitinase Al from Bacillus circulans WL-12 was crystallized by vapor-diffusion technique. The crystals belong to the triclinic space group P1 with cell dimensions a = 43.96Å, b = 48.62Å, c = 54.59Å, a =108.90°, b =95.06°, and g = 115.77°, and contain one molecule in the asymmetric unit. High-quality diffraction data were collected at 20°C with radiation from a synchrotron source up to 1.5Å resolution.

[Back to top] Purification and Crystallization of a Catechol 2,3-Dioxygenase PheB from Bacillus stearothermophilus BR219. Keisuko Sugimoto, Toshiya Senda, Eiji Masai, Kazuhide Kimbara, Masao Fukuda and Yukio Mitsui.
The thermostable catechol 2,3-dioxygenase from Bacillus stearothermophilus BR219 has been crystallized by vapor-diffusion method. The crystals were grown from a solution containing isopropanol, HEPES and magnesium chloride. The crystals belonged to the monoclinic system with a space group P2₁ and unit cell dimensions of a=69.4Å, b=61 .5Å, c=153. lÅ and b=92.6°.

[Back to top] Crystallization and Preliminary X-ray Crystallographic Studies of Ribonuclease LE from Lycopersicon esculentum. Nobutada Tanaka, Jun Arai, Norio Inokuchi, Takashi Koyama, Kazuko Ohgi, Masachika Irie and Kazuo T. Nakamura.
The ribonuclease LE, a plant ribonuclease from Lycopersicon esculentum, has been crystallized by the hanging-drop vapour diffusion method using polyethylene glycol 1,540 as the precipitating agent. The crystals belong to an orthorhombic space group P2₁2₁2₁ with cell dimensions of a = 74.10Å, b = 78.72 Å, and c = 33.00 Å. There is one molecule per asymmetric unit. The crystals diffract to at least 2.0 Å resolution and are suitable for X-ray structure analysis at high resolution.