Tolerance of Protein Structures to the Changes of Amino Acid Sequences
and Their Interactions. The Nature of the Folding Code. Pp. 115-130.
Alexander P. Demchenko and Vladimir A. Chinarov
[Abstract]
Regular Papers
De Novo Design and CD Studies of Model b-Sheet
Peptides. Pp. 131-136.
Yinlin Sha, Yinling Li, Qi Wang, Keqiatig Fan, Dongsheng Liu, Luhua
Lai and Youqi Tang
[Abstract]
CD Evidence of a Peptide Ongoing a/b/Random
Transition in Different Solutions. Pp. 137-140.
Yinlin Sha, Yinling Li, Qi Wang, Keqiang Fan, Dongsheng Liu, Luhua
Lai and Youqi Tang
[Abstract]
Nanoparticle Formation of Self-Assembling Two-a-Helix
Peptide Induced by Heme-Binding. Pp. 141-144.
Ikuo Obataya, Seiji Sakamoto, Akihiko Ueno and Hisakazu Mihara
[Abstract]
Flexible Synthesis of Symmetric and Non-Symmetric HIV-I Protease Inhibitors
Based on ALL-S-Diaminodiol Isosteres. Pp. 145-148.
Alessandro Tossi, Nikolinka Antcheva, Fabio Benedetti, Stefano Norbedo,
Stanislav Miertus and Domenico Romeo
[Abstract]
19F NMR Study of the Binding of Fluorinated Diethylstibestrol
to the Human Estrogen Receptor. Pp. 149-154.
Matthew C. Skeels, Branka Salopek Sondi and Linda A. Luck
[Abstract]
Microwave Exposure Effect on a Thermophilic Alcohol Dehydrogenase. Pp.
155-162.
La Cara, F., D'Auria, S., Scarfi, M.R., Zeni, 0., Massa, R., d'Ambrosio,
G., Franceschetti, G., De Rosa, M. and Rossi, M.
[Abstract]
Specificity of the Vatairea macrocarpa Lectin Towards Glycans
Exhibiting Exposed Gal/GalNAc Residues. Pp. 163-172.
Marcio V. Ramos, Benildo S. Cavada, Juan J. Calvete, Alexandre H.
Sampaio, Anne M. Mazard, Anick Barre, Thalles B. Grangeiro, Beatriz T.
Freitas, Katia B. Leite and Pierre Rouge
[Abstract]
Inactivated Actin, An Aggregate Comprised of Partially-Folded Monomers,
Has an Overall Native-Like Packing Density. Pp. 173-178.
Irma M. Kuznetsova, Konstantin K. Turoverov and Vladimir N. Uversky
[Abstract]
Autoantibodies with Amylolytic Activity. Pp. 179-184.
Andrew N. Savel'ev, Elena V. Eneyskaya, Konstantin A. Shabalin,
Michael V. Filatov and Kirill N. Neustroev
[Abstract]
[Back to top] De Novo
Design and CD Studies of Model b-Sheet Peptides.
Yinlin Sha, Yinling Li, Qi Wang, Keqiatig Fan, Dongsheng Liu, Luhua Lai
and Youqi Tang.
Two nine-residue peptide sequences (al, a2) with [(Hb-Hb-Hp-Hp)-Hb-(Hp-Hp-Rb-Hb)]
(Hb, hydrophobic residue, Hp, hydrophilic residue) pattern were synthesized
by solid phase peptide synthesis protocol and purified by RP-HPLC. The
CD spectrum of al in water shows a positive near 196.5nm and a negative
at ca 216.5nm, which have been considered as the characteristics of b-sheet.
The characteristic of a2 curve, a negative near 213nm and a shoulder at
199nm has been postulated as the contribution from b-sheet
mixed with random coil. The peptide al is also characterized by chemical
and thermal denaturations.
[Back to top] CD Evidence
of a Peptide Ongoing a/b/Random Transition in
Different Solutions. Yinlin Sha, Yinling Li, Qi Wang, Keqiang Fan, Dongsheng
Liu, Luhua Lai and Youqi Tang.
Conformational transition is a very interesting topic of solution of
protein aggregation and amyloid formation. The design, synthesis, purification
and conformational studies of a nine-residue peptide (LLEELKEVL, name al)
in water have been discussed recently [1]. Here we report the confirmational
transitions of al in different solutions. In water or in TFE the CD spectrum
shows a maximum at 198nm and a minimum at 217nm, a typical characteristic
of b-sheet. A negative maximum at ca. I 98nm
is observed in PBS (pH 7.02), which have been concluded as the characteristics
of random coil. With the titration of SDS solution (5%-10%), the negative
near 207 and 222nm are enhanced, which means the helix component increases.
The thermal denaturation studies of al in TFE or in SDS indicate the oligomerization
of the peptide.
[Back to top] Nanoparticle
Formation of Self-Assembling Two-a-Helix Peptide
Induced by Heme-Binding. Ikuo Obataya, Seiji Sakamoto, Akihiko Ueno and
Hisakazu Mihara.
A designed two-a-helix peptide H6-2a
bound effectively Fe(III)-mesoporphyrin (heme) and the heme-binding simultaneously
induced the formation of nanoparticles. Thus, new self-assembling system
of peptide with heme was accomplished.
[Back to top] Flexible
Synthesis of Symmetric and Non-Symmetric HIV-I Protease Inhibitors Based
on ALL-S-Diaminodiol Isosteres. Alessandro Tossi, Nikolinka Antcheva, Fabio
Benedetti, Stefano Norbedo, Stanislav Miertus and Domenico Romeo.
C2 symmetric and non-symmetric pseudopeptide inhibitors
of HIV-1 protease, containing S,S,S,S,-diaminodiol isostere have
been obtained by a synthetic strategy designed to couple a high degree
of stereochemical control with complete flexibility in the choice of residues
in the central core and flanking chains. Using this approach, inhibitors
with 1C50 values in the low nanomolar range were assembled from
readily available aminoacids and carboxylic acids, chosen with the aid
of molecular modelling.
[Back to top] 19F
NMR Study of the Binding of Fluorinated Diethylstibestrol to the Human
Estrogen Receptor. Matthew C. Skeels, Branka Salopek Sondi and Linda A.
Luck.
In this paper we report the binding of hexafluorodiethylstibestrol
to two constructs of the recombinant hormone-binding domain of the human
estrogen receptor produced in E. coli. Our fluorine NMR studies
have shown the protein to selectively bind the E-isomer and the NMR signals
show protein-induced shifts.
[Back to top] Microwave
Exposure Effect on a Thermophilic Alcohol Dehydrogenase. La Cara, F., D'Auria,
S., Scarfi, M.R., Zeni, 0., Massa, R., d'Ambrosio, G., Franceschetti, G.,
De Rosa, M. and Rossi, M.
It has been studied the effect of microwave irradiation on the thermostable
alcohol dehydrogenase isolated from the Archaeon Sulfolobus solfataricus
in order to discriminate between thermal and non-thermal effects of such
non-ionizing radiations on protein's features. The results indicate a non-thermal
effect of microwave on the structural and functional properties of the
enzyme as well as the dependence of the enzyme stability from the protein
concentration.
[Back to top] Specificity
of the Vatairea macrocarpa Lectin Towards Glycans Exhibiting Exposed Gal/GalNAc
Residues. Marcio V. Ramos, Benildo S. Cavada, Juan J. Calvete, Alexandre
H. Sampaio, Anne M. Mazard, Anick Barre, Thalles B. Grangeiro, Beatriz
T. Freitas, Katia B. Leite and Pierre Rouge.
The binding specificity of the lectin from Vatairea macrocarpa,
a legume from tribe Dalbergieae, was investigated by surface plasmon
resonance measurements and molecular modelling and docking. The lectin
is a Gal/GalNac-specific protein which readily interacts with both N-
and O-linked glycans. It resembles other legume lectins from the
closely related tribe Sophoreae characterized so far. Its specific
interaction with glycoproteins should allow its use as a tool for both
the isolation and characterization of various N- and O- linked
glycoconjugates.
[Back to top] Inactivated
Actin, An Aggregate Comprised of Partially-Folded Monomers, Has an Overall
Native-Like Packing Density. Irma M. Kuznetsova, Konstantin K. Turoverov
and Vladimir N. Uversky.
The packing density of inactivated actin was analyzed by comparison
of "apparent" molecular mass, Mapp, (measured by gel-filtration
column, calibrated by native proteins with known molecular masses) with
the "true" value of this parameter, Mtrue (calculated from the
Stokes radius, RS, and sedimentation constant, s). The determined
values were comparable reflecting the fact that packing density of the
inactivated actin is rather close to that of native proteins.
[Back to top] Autoantibodies
with Amylolytic Activity. Andrew N. Savel'ev, Elena V. Eneyskaya, Konstantin
A. Shabalin, Michael V. Filatov and Kirill N. Neustroev.
Hydrolytic activity toward maltooligosaccharides was found in the human
IgG fraction purified by affinity chromatography with protein G-Sepharose
followed by ion-exchange and gel-permeation chromatography. The IgG Fab
was shown to retain the amylolytic activity. Amylolytic activity of the
IgG fraction from pregnant donors was 50 fold higher than from normal donors.
Increased amylolytic activity of the IgG fraction was detected in blood
from oncological donors.