Carboxyl-Terminal Sequencing: New C-Terminal Peptidyl-Thiohydantoins
Formation Conditions. Pp. 251-256.
Patricia D. Ribeiro, Ronaldo S.M. Borges, Paulo R.R. Costa, Elias
W. Alves and Olga L T. Machado
[Abstract]
Sodium Iodide as a Novel, Neutral and Facile Deprotecting Reagent of
N-tert-Butyloxycarbonyl
Groups in Peptide Chemistry. Pp. 257-258.
Jungyeob Ham, Kyungseok Choi, Jaeyoung Ko, Hanwon Lee and Mankil
Jung
[Abstract]
Designing b-Hairpin Forming Short Peptide.
Pp. 259-264.
Sha Yinlin, Huang Yongliang, Wang Qi and Lai Luhua
[Abstract]
Compression Refolding of Cytochrome C. Pp. 265-268.
Masashi Dewa, Masato Tayauchi, Masao Sakurai and Katsutoshi Nitta
[Abstract]
New Synthetic Peptides on Nuclear Localization Signal Derived from Jun
by Single Amino Acid Substitutions. Pp. 269-272.
Kazuhiro Chida, Tomoko Tagawa, Shushi Nagamori and Toshio Kuroki
[Abstract]
Soluble Expression and One-Step Purification of Recombinant Bacillus
anthracis Protective Antigen. Pp. 273-278.
David C. Willhite and Steven R. Blanke
[Abstract]
Effect of Alcohol on Aggregation of Human Neuronal Tau Protein. Pp.
279-286.
Rong-Qiao He, Jian-Ying Luo and Wei Li
[Abstract]
In Vitro Effects of a Novel Tetrapeptide in Human Neutrophils and in
a Rat Model of Osteoarthritis. Pp. 287-294.
Satish Devadas, C. V. Ramesh and R. Puvanakrishnan
[Abstract]
a-Fetoprotein Structure Depends on the Protein
Purification Procedure: Further Evidence on the Structure Forming Role
of the Ligands. Pp. 295-301.
Andrey Yu Tomashevski, Natalya V. Narishneva, Tatyana N. Melnik
and Vladimir N. Uversky
[Abstract]
[Back to top] Carboxyl-Terminal
Sequencing: New C-Terminal Peptidyl-Thiohydantoins Formation Conditions.
Patricia D. Ribeiro, Ronaldo S.M. Borges, Paulo R.R. Costa, Elias W. Alves
and Olga L T. Machado.
The present study explores conditions to activate the carboxyl group
before the coupling of C-terminus-AA with TMS-ITC. N-tert-butoxy-carbonyl
amino acids (Boc-AAs) and Leucine Enkephalin were used as models and isobutyl
chloroformate was used as a C-terminal activator. The reaction coupling
activated AA with TMS-ITC was temperature dependent. We also report here
a new, efficient, economical and ecological technique to separate the mixture
of amino acids thiohydantoins (TH-AA).
[Back to top] Sodium Iodide
as a Novel, Neutral and Facile Deprotecting Reagent of N-tert-Butyloxycarbonyl
Groups in Peptide Chemistry. Jungyeob Ham, Kyungseok Choi, Jaeyoung Ko,
Hanwon Lee and Mankil Jung.
The N-tert-butyloxycarbonyl (N-t-Boc) protecting groups
of amino acids were cleanly and easily removed by treatment with sodium
iodide under neutral conditions.
[Back to top] Designing
b-Hairpin Forming Short Peptide. Sha Yinlin,
Huang Yongliang, Wang Qi and Lai Luhua.
The short linear peptide sequence H2N-Val-Thr-Leu-D-Pro-Gly-Val-Thr-Val-COOH
predicted to form b-hairpin was synthesized
by Fmoc/Bu strategy and purified by RP-HPLC. The CD spectra show a minimum
at ca. 216nm and a maximum at ca. 194nm, which have been concluded as the
common contribution from b-turn and b-sheet,
and the structure in water was enhanced by organic reagent, such as TFE,
acetonitrile and isopropyl alcohol.
[Back to top] Compression
Refolding of Cytochrome C. Masashi Dewa, Masato Tayauchi, Masao Sakurai
and Katsutoshi Nitta.
Perturbation of thermal unfolding of cytochrome C with compression
was investigated to obtain volumetric quantities of the unfolding.
At pH 2.9-3.2 and around 40-60ºC, cytochrome C does not unfold but
refold when compressed. This phenomenon contradicts to our present
understanding that a protein unfolds if high pressure is applied.
The volume change is strongly dependent on temperature and decreases with
decreasing temperature. This ckiange of volume changes its sign around
40ºC and is negative at room temperature.
[Back to top] New Synthetic
Peptides on Nuclear Localization Signal Derived from Jun by Single Amino
Acid Substitutions. Kazuhiro Chida, Tomoko Tagawa, Shushi Nagamori and
Toshio Kuroki.
We examined nuclear transport activities of synthetic peptides on the
basis of nuclear localization signal (NLS) of Jun, Arg-Lys-Arg-Lys-Leu,
by microinjection into the cytoplasm of NRK cells. Each amino acids of
this sequence was replaced by protein or nonprotein amino acids. The four
basic amino acids could be replaced by either lysine, arginine or ornithine
(Orn). Replacement of the leucine by a methionine enhanced the transport
activity. A nonprotein amino acid sequence Orn-Orn-Orn-Orn-Nrv (norvaline)
functioned as an NLS.
[Back to top] Soluble
Expression and One-Step Purification of Recombinant Bacillus anthracis
Protective Antigen. David C. Willhite and Steven R. Blanke.
We have greatly simplified production of the Bacillus anthracis
protective antigen (PA), the immunoprotective antigen of the anthrax vaccine.
By varying induction conditions, we have expressed stable, soluble PA in
E. coli, affinity-tagged to facilitate rapid, single-step purification.
Recombinant PA exhibited identical properties to B. anthracis PA.
Our approach is an attractive strategy for generating purified vaccine
antigens that are difficult to express recombinantly.
[Back to top] Effect of
Alcohol on Aggregation of Human Neuronal Tau Protein. Rong-Qiao He, Jian-Ying
Luo and Wei Li.
Effects of alcohol and heparin on aggregation of the recombinant tau
have been studied. Alcohol at low concentrations induces tau polymerization
distinguishably at room temperature and 37ºC. The effect of heparin
on tau's aggregation was cooperative with that of alcohol if both heparin
and alcohol were added to tau solutions. It appears that the polymerization
of tau might be correlated to the disorder of neuronal transportation of
alcoholism.
[Back to top] In Vitro
Effects of a Novel Tetrapeptide in Human Neutrophils and in a Rat Model
of Osteoarthritis. Satish Devadas, C. V. Ramesh and R. Puvanakrishnan.
PEP1261, a derivative of Lys-Arg-Asp-Ser (KRDS) exhibits an inverse
dose response in that it exhibits antioxidant properties at low concentrations
and oxidant characteristics at higher concentrations. This study shows
that when PEP1261 is tested on neutrophils, it exhibits marked inhibition
on myeloperoxidase activity and also decreases the levels of H202
and superoxide. This indicates therapeutic application for PEP1261 in osteoarthritis.
[Back to top] a-Fetoprotein
Structure Depends on the Protein Purification Procedure: Further Evidence
on the Structure Forming Role of the Ligands. Andrey Yu Tomashevski, Natalya
V. Narishneva, Tatyana N. Melnik and Vladimir N. Uversky.
a-Fetoprotein samples isolated from human
cord serum by metal affinity chromatography and immunoaffinity method were
compared by circular dichroism, fluorescence spectroscopy and scanning
microcalorimetry. The isolation procedures were quite distinguished by
their influence on native protein structure (and, consequently, by the
effectiveness of natural ligand release from a protein molecule). As a
result, structural properties and conformational stability of a-fetoprotein
in the samples were found to be rather different.