A consensus zinc finger peptide: design, high-affinity metal binding, a pH-dependent structure, and a His to Cys sequence variant

1991 ◽  
Vol 113 (12) ◽  
pp. 4518-4523 ◽  
Author(s):  
Beth Allyn Krizek ◽  
Barbara T. Amann ◽  
Valda J. Kilfoil ◽  
Denise L. Merkle ◽  
Jeremy M. Berg
Keyword(s):  
Zinc Finger ◽  
Metal Binding ◽  
Sequence Variant ◽  
Peptide Design ◽  
High Affinity ◽  
Ph Dependent ◽  
Zinc Finger Peptide

Metal binding to a zinc-finger peptide: a comparison between solution and the gas phase

2011 ◽  
Vol 47 (1) ◽  
pp. 412-414 ◽  
Author(s):  
Yana Berezovskaya ◽  
Craig T. Armstrong ◽  
Aimee L. Boyle ◽  
Massimiliano Porrini ◽  
Derek N. Woolfson ◽  
...  
Keyword(s):  
Gas Phase ◽  
Zinc Finger ◽  
Metal Binding ◽  
Zinc Finger Peptide

scholarly journals Metal binding and folding properties of a minimalist Cys2His2 zinc finger peptide.

1992 ◽  
Vol 89 (11) ◽  
pp. 4796-4800 ◽  
Author(s):  
S. F. Michael ◽  
V. J. Kilfoil ◽  
M. H. Schmidt ◽  
B. T. Amann ◽  
J. M. Berg
Keyword(s):  
Zinc Finger ◽  
Metal Binding ◽  
Zinc Finger Peptide

Kinetics of metal binding by a zinc finger peptide

2000 ◽  
Vol 297 (1-2) ◽  
pp. 217-219 ◽  
Author(s):  
Jeffrey C Buchsbaum ◽  
Jeremy M Berg
Keyword(s):  
Zinc Finger ◽  
Metal Binding ◽  
Zinc Finger Peptide ◽  
Kinetics Of

scholarly journals Metal binding spectrum and model structure of theBacillus anthracisvirulence determinant MntA

Metallomics ◽  
2015 ◽  
Vol 7 (10) ◽  
pp. 1407-1419 ◽  
Author(s):  
Elena Vigonsky ◽  
Inbar Fish ◽  
Nurit Livnat-Levanon ◽  
Elena Ovcharenko ◽  
Nir Ben-Tal ◽  
...  
Keyword(s):  
Bacillus Anthracis ◽  
Metal Binding ◽  
Model Structure ◽  
High Affinity ◽  
Virulence Determinant ◽  
System P

TheBacillus anthracisvirulence determinant MntA is a high-affinity manganese system.

scholarly journals In vivo anti-influenza virus activity of a zinc finger peptide.

1997 ◽  
Vol 41 (3) ◽  
pp. 687-692 ◽  
Author(s):  
A K Judd ◽  
A Sanchez ◽  
D J Bucher ◽  
J H Huffman ◽  
K Bailey ◽  
...  
Keyword(s):  
Amino Acids ◽  
Influenza Virus ◽  
Amino Acid ◽  
Virus Infection ◽  
Zinc Finger ◽  
Matrix Protein ◽  
H3n2 Virus ◽  
Arterial Oxygen ◽  
Treatment Schedule ◽  
Zinc Finger Peptide

Matrix protein (M1) is a major structural protein of influenza virus, and it inhibits its own polymerase. A 19-amino-acid peptide, corresponding to a zinc finger region of the M1 sequence of influenza virus strain A/PR/8/34 (H1N1), centered around amino acids 148 to 166, was synthesized. This peptide, designated peptide 6, represents a zinc finger which includes a 7-amino-acid loop or finger and a 4-amino-acid tail at the carboxyl terminus, in addition to the 8 amino acids involved in the coordination of Zn. Three experiments were run to evaluate the activity of peptide 6 on infections induced in mice by influenza A/PR/8/34 and A/Victoria/3/75 (H3N2) viruses. Intranasal (i.n.) treatment of the H1N1 virus infection with 30 or 60 mg/kg of body weight/day, three times daily for 5 days, beginning 4 h pre-or 8 h post-virus exposure, was effective in preventing death, reducing the arterial oxygen decline, and inhibiting lung consolidation. Virus titers in the lungs determined on day 5 were reduced by up to 1.5 log10 in treated groups, but considerable variation in the titers of the recovered virus was seen. The H3N2 virus infection was treated i.n. with 30, 60, or 120 mg of peptide 6/kg/day by using the above-mentioned delayed initiation treatment schedule, and similar protection was seen, although lung virus titers were not reduced in the day-5 assay. Peptide 6 was well tolerated at doses up to 60 mg/kg/day. This zinc finger peptide may provide a new class of antivirals effective against influenza virus.

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