scholarly journals Halogenation at the Phenylalanine Residue of Monomethyl Auristatin F Leads to a Favorable cis/trans Equilibrium and Retained Cytotoxicity

2021 ◽  
Author(s):  
Iris K. Sokka ◽  
Surachet Imlimthan ◽  
Mirkka Sarparanta ◽  
Hannu Maaheimo ◽  
Mikael P. Johansson ◽  
...  
Keyword(s):  
Phenylalanine Residue

Frequency of the delta Phe508 mutation and correlation with XV.2c/KM-19 haplotypes in an American population of cystic fibrosis patients: results of a collaborative study

1990 ◽  
Vol 36 (10) ◽  
pp. 1741-1746 ◽  
Author(s):  
W E Highsmith ◽  
G L Chong ◽  
H T Orr ◽  
T R Perry ◽  
D Schald ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Haplotype Analysis ◽  
Screening Program ◽  
Collaborative Study ◽  
Population Based ◽  
Carrier Status ◽  
Chain Reaction ◽  
Polymerase Chain ◽  
Phenylalanine Residue ◽  
Test Result

Abstract The cystic fibrosis (CF) gene has been recently cloned, and a deletion of 3 basepairs (bp) of DNA was found on most of the CF chromosomes. This deletion leads to the synthesis of a protein that lacks a phenylalanine residue at position 508. Using two polymerase chain reaction protocols to study the frequency of this mutation in a series of 192 CF patients, we found the mutation on 72% of affected chromosomes. We then used this value to calculate the predictive value of a negative test result in a population-based screening program for CF carrier status. Haplotype analysis with the polymorphic markers XV.2c and KM-19 on 239 CF chromosomes revealed that 90.7% of CF chromosomes with the deletion had a single haplotype. This haplotype was also associated with 60.4% of CF chromosomes with unknown mutations. These values can be used to calculate the probability of whether an individual from the general population is a carrier of any CF mutation.

scholarly journals A Cation-  Interaction in the Binding Site of the Glycine Receptor Is Mediated by a Phenylalanine Residue

2008 ◽  
Vol 28 (43) ◽  
pp. 10937-10942 ◽  
Author(s):  
S. A. Pless ◽  
K. S. Millen ◽  
A. P. Hanek ◽  
J. W. Lynch ◽  
H. A. Lester ◽  
...  
Keyword(s):  
Binding Site ◽  
Glycine Receptor ◽  
Phenylalanine Residue

scholarly journals The Aromatic Ring of Phenylalanine 334 Is Essential for Oligomerization of Vibrio vulnificus Hemolysin

2009 ◽  
Vol 192 (2) ◽  
pp. 568-574 ◽  
Author(s):  
Takashige Kashimoto ◽  
Shunji Ueno ◽  
Takeshi Koga ◽  
Shinji Fukudome ◽  
Hayato Ehara ◽  
...  
Keyword(s):  
Aromatic Ring ◽  
Vibrio Vulnificus ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Binding Activity ◽  
Gram Negative Bacteria ◽  
Ovary Cells ◽  
In The Wild ◽  
And Function ◽  
Phenylalanine Residue

ABSTRACT Vibrio vulnificus hemolysin (VVH) is thought to be a member of the cholesterol-dependent cytolysin (CDC) family of pore-forming toxins. To date, the structure-function relationships of CDCs produced by Gram-negative bacteria remain largely unknown. We show here that the aromatic ring of phenylalanine residue conserved in Vibrionaceae hemolysins is essential for oligomerization of VVH. We generated the VVH mutants; substituted Phe 334 for Ile (F334I), Ala (F334A), Tyr (F334Y), or Trp (F334W); and tested their binding and oligomerizing activity on Chinese hamster ovary cells. Binding in all mutants fell by approximately 50% compared with that in the wild type. Oligomerizing activities were completely eliminated in F334I and F334A mutants, whereas this ability was partially retained in F334Y and F334W mutants. These findings indicate that both hydrophobicity and an aromatic ring residue at the 334th position were needed for full binding activity and that the oligomerizing activity of this toxin was dependent on the existence of an aromatic ring residue at the 334th position. Our findings might help further understanding of the structure-and-function relationships in Vibrionaceae hemolysins.

scholarly journals Transformation of NIH 3T3 fibroblasts by an activated form of p59hck.

1989 ◽  
Vol 9 (6) ◽  
pp. 2724-2727 ◽  
Author(s):  
S F Ziegler ◽  
S D Levin ◽  
R M Perlmutter
Keyword(s):  
Tyrosine Kinases ◽  
Soft Agar ◽  
Protein Tyrosine Kinases ◽  
3T3 Fibroblasts ◽  
Family Protein ◽  
Cloning Assay ◽  
Transforming Activity ◽  
Nih 3T3 ◽  
Soft Agar Cloning ◽  
Phenylalanine Residue

Phosphorylation of a tyrosine residue near the carboxy terminus of src-family protein tyrosine kinases is believed to regulate the biological activity of these gene products. Conversion of this tyrosine in p59hck (Tyr-501) to a phenylalanine residue by using oligonucleotide-directed mutagenesis yielded a product (p59hckF501) with very potent transforming activity. Quantitative analysis by a soft-agar cloning assay revealed that p59hckF501 was more than 100-fold more effective than a closely related transforming element, p56lckF505, in colony formation. Cells bearing p59hckF501 had increased levels of protein phosphotyrosine. The ability of p59hckF501 to transform NIH 3T3 cells was abolished by a second mutation believed to destroy the ATP-binding domain.

A new CCK analogue differentiates two functionally distinct CCK receptors in rat and mouse pancreatic acini

1989 ◽  
Vol 257 (4) ◽  
pp. G594-G600 ◽  
Author(s):  
T. Matozaki ◽  
J. Martinez ◽  
J. A. Williams
Keyword(s):  
Competitive Inhibition ◽  
Inhibitory Effect ◽  
Leucine Incorporation ◽  
Amylase Release ◽  
Pancreatic Acini ◽  
Cck Receptors ◽  
Partial Agonists ◽  
Low Concentrations ◽  
Phenylalanine Residue ◽  
Stimulation Of

Analysis of the competitive inhibition of 125I-labeled cholecystokinin octapeptide (CCK-8) binding to isolated rat or mouse pancreatic acini showed that in both species CCK-8 interacts with two different affinity sites. A newly synthesized CCK analogue modified at the COOH-terminal phenylalanine residue totally inhibited 125I-CCK binding. This interaction occurred with sites of a single affinity in rat acini but with two different affinity sites in mouse acini. When acini were incubated with increasing concentrations of CCK-8, a biphasic stimulation of amylase release was observed. By use of rat acini, the analogs stimulated amylase release but caused no inhibition at supramaximal concentrations. By contrast, in mouse pancreatic acini, analogues showed a biphasic stimulation of amylase release similar to CCK-8. Both CCK-8 and the analogue stimulated [3H]leucine incorporation into protein at low concentrations in rat pancreatic acini. Higher concentrations of CCK-8 profoundly inhibited [3H]leucine incorporation, whereas the analogue had no inhibitory effect. Moreover, the analogue at higher concentrations blocked the inhibition of [3H]leucine incorporation caused by CCK-8 but did not affect carbamylcholine-induced inhibition. In mouse acini, however, the CCK analogue inhibited [3H]leucine incorporation similar to the effect of CCK-8. The results support the concept that occupancy of distinct affinity sites or states of the CCK receptor is associated with specific biological actions. A model of the CCK receptor is proposed in which two interchangeable affinity states exist. By occupying all the receptors in only one state, the new CCK analogues serve as partial agonists of some and antagonists of other actions of CCK.

scholarly journals Semisynthetic human [[3H2]Phe1]proinsulin

1987 ◽  
Vol 247 (3) ◽  
pp. 785-788 ◽  
Author(s):  
R M L Jones ◽  
K Rose ◽  
R E Offord
Keyword(s):  
Time Course ◽  
Recombinant Dna ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Specific Radioactivity ◽  
Reversed Phase ◽  
British Library ◽  
Recombinant Dna Techniques ◽  
Phenylalanine Residue

Biosynthetic human proinsulin (obtained by recombinant DNA techniques) was used as the starting material for the preparation, by semisynthetic methods, of [3H]proinsulin with the label at the N-terminal phenylalanine residue. The labelled proinsulin was characterized by its retention time on reversed-phase h.p.l.c., by polyacrylamide-gel electrophoresis, by the time course of its enzymic conversion into insulin and by chromatographic analysis after extensive proteolytic degradation. The specific radioactivity of the product was 5 Ci/mmol. Experimental details of the preparation of human [[3H]Phe1]proinsulin, the isolation of this product by isocratic h.p.l.c. and gel filtration, and further characterization of protein intermediates have been deposited as supplement SUP 50138 (12 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on prepayment [see Biochem. J. (1987) 241, 5].

scholarly journals Synthesis of bradykinin fragments and their analogs modified at a phenylalanine residue.

1980 ◽  
Vol 28 (1) ◽  
pp. 310-313 ◽  
Author(s):  
YOSHIO OKADA ◽  
YUKO TSUKA ◽  
MASAMI YAGYU
Keyword(s):  
Phenylalanine Residue

Renin inhibitors. Dipeptide analogs of angiotensinogen utilizing a structurally modified phenylalanine residue to impart proteolytic stability

1988 ◽  
Vol 31 (12) ◽  
pp. 2277-2288 ◽  
Author(s):  
Jacob J. Plattner ◽  
Patrick A. Marcotte ◽  
Hollis D. Kleinert ◽  
Herman H. Stein ◽  
Jonathan Greer ◽  
...  
Keyword(s):  
Renin Inhibitors ◽  
Proteolytic Stability ◽  
Phenylalanine Residue

Peptide Conformations. I. Nuclear Magnetic Resonance Study of the Carbamate Reaction of Amino Acids and Peptides

1971 ◽  
Vol 49 (5) ◽  
pp. 767-776 ◽  
Author(s):  
R. U. Lemieux ◽  
M. A. Barton
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Nuclear Magnetic Resonance Study ◽  
Amide Bond ◽  
Resonance Spectroscopy ◽  
Peptide Conformations ◽  
End Distance ◽  
Phenylalanine Residue ◽  
Nuclear Magnetic

Nuclear magnetic resonance spectroscopy has been applied to the study of carbamate formation in solutions of amino acids and peptides in a carbonate-bicarbonate system. The possible conformations of these carbamates are discussed in terms of the n.m.r. data obtained. The n.m.r. parameters are reported for the diastereomers L-alanyl-L or D-phenylalanine and L-phenylalanyl-L or D-alanine and for the dipeptide glycyl-L-phenylalanine and their carbamates. The results are interpreted in terms of preferred rotamers about the Cα—Cβ bond of the phenylalanine residue and a β-type conformation of the peptide chain, wherein the two α-protons lie in the plane of the amide bond. All observations are in agreement with a shorter end to end distance in L,D- compared with L,L-dipeptides.

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