xt7nzs2k9f04 https://exploreuk.uky.edu/dips/xt7nzs2k9f04/data/mets.xml University of Kentucky University of Kentucky Chemistry Department 1990-04-16 A brochure for the Naff Symposium, an event hosted by the University of Kentucky Chemistry Department supported by the Anna S. Naff Endowment Fund. This brochure belongs to the University of Kentucky Chemistry Department Records collection, accession number 2014ua075. archival material  English University of Kentucky Chemistry Department Contact the Special Collections Research Center for information regarding rights and use of this collection. University of Kentucky Chemistry Department Naff Symposium brochures Sixteenth Annual Symposium on Chemistry and Molecular Biology: "Molecular Recognition" text Sixteenth Annual Symposium on Chemistry and Molecular Biology: "Molecular Recognition" 1990 1990-04-16 2026 true xt7nzs2k9f04 section xt7nzs2k9f04  

1990 PROGRAM

 

Registration and Coffee—Room 137,
Chemistry-Physics Building

Welcome by Dr. Robert Hemenway,
Chancellor, University of Kentucky, Room
139, Chemistry-Physics Building

Introductory Remarks

Dr. Andrew D. Hamilton, University of
Pittsburgh

New Artificial Receptors for Complexation
and Catalysis

An important goal in modern bioorganic chemistry concerns
the design of synthetic molecules that mimic various aspects of
enzyme chemistry. Detailed study of such models can lead not
only to insights into the nature of enzyme action but also to new
chemical species with some of the specificity and speed normally
associated only with enzymes. Our approach has been to focus
on biologically significant substrates and to construct complemen-
tary receptors containing multiple binding interactions. In particular,
we have incorporated several hydrogen bonding sites into a
macrocyclic framework to provide a highly selective receptor for
barbiturates. The approach has been extended to other substrates
including urea, small peptides and the different nucleotide bases.
Artificial receptors of this type may lead to the development of
novel pharmaceutical strategies, drug delivery systems or chemical
sensor designs.

1 0:45 Discussion

10:50 Dr. William F. DeGrado, Central Research
and Development Dept., E.I. du Pont de
Nemours and Co.

De Novo Design of Helical Proteins.

Our group has recently adopted a synthetic approach to
understanding the structural basis for protein function. In order
to test some of the rules and concepts which are believed to be
important for protein folding and stability we are attempting to
design some simple proteins which should fold into predetermined
three-dimensional structures. Two types of helical proteins have
been designed: the first is an idealized version of a four-helix bun—
dle, a folding pattern found in the structures of a variety of natural
water-soluble proteins including myohemerythrin, cytochrome C,
and apoferittin, while the other class of designed proteins is meant
to mimic the structures of proteins which form ion channels such
as the acetylcholine receptor. The synthesis and characterization
of these proteins are currently underway and will be the focus of
the talk.

1 1:50 Discussion

Buffet Lunch, Faculty Club (Please return
card by April 7, 1990 for reservations. Cost
$6.00 to be paid at registration.)

Dr. Steven C. Zimmerman, University of
Illinois

Chemically Synthesized Mimics of Biological
Receptors and Enzyme Catalysts.

Noncovalent interactions are of fundamental importance to all
biological processes. The efficiency of enzymatic catalysis and the
binding specificity of antibodies depends upon a large number of
complementary intermolecular contacts. A promising approach
to understanding the nature of these noncovalent interactions is
through the study of chemical model systems. In this laboratory
we have studied models for both biological “receptors” and for
enzymic catalysis. The synthetic receptors have been designed to
complex aromatic substrates using only aromatic 1r-stacking in-
teractions, or a combination of 7r-stacking interactions and
hydrogen bonding. These studies have shown that a very high
degree of cooperativity can be obtained between multiple binding
interactions. We have also developed a new model of the histidine-
aspartate couple which contains a syn oriented carboxylate. Several
enzymes, which have evolved independently, have been found
to contain aspartic acid residues hydrogen bonded to catalytical-
ly active histidine residues. Previous small molecule mimics of the
His-Asp couple have constrained the carboxylate to an anti orienv
tation, while only the syn orientation is found in the enzymatic
system.

2:40 Discussion

2:50 Dr. Ronald Breslow, Columbia University
Geometric Control of Binding and Catalysis

Multipoint binding interactions lead to increased affinity and
multifunctional catalysis leads to increased rates. Both can pro»
duce increased selectivities for substrates and products. Examples
from the first area include ditopic binders with antibody-like af-
finities, and ditopic functionalizing catalysts. Examples from the
latter area include examples in which bifunctional catalysis is
geometrically controlled in transaminase and ribonuclease mimics.
Rigid binding can be useful for rate accelerations, but some
freedom of motion must be left so the molecular complex can adapt
to the changing geometric demands of the reaction path. We will
describe an example of the rate improvement that this principle
leads to.

3:50 Discussion
4:00 Mixer.

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Sixteenth Annual
Symposium on

Chemistry
&
Molecular

established in the memory of
Anna S. Naff

 

MOLECULAR
RECOGNITION

 

SPEAKERS

Ronald Breslow
William F. DeGrado
Andrew D. Hamilton

Steven C. Zimmerman

Monday, April 16, 1990
Department of Chemistry

University of Kentucky
Lexington, Kentucky 40506—0055

 

 Sixteenth Annual Symposium on

Chemistry &
Molecular Biology

established in the memory of Anna S. Naff

Monday, April 16, 1990, 9:00 a.m.
Chemistry-Physics Building—Room 139

Department of Chemistry,

University of Kentucky

 

MOLECULAR RECOGNITION

 

Ronald Breslow, Ph.D., Harvard Univer-
sity. S.L. Mitchill Professor of Chemistry, Col-
umbia University. Member of the National
Academy of Sciences, the American Academy
of Arts and Sciences, and the American
Philosophical Society. Recipient of: Centenary
Medal from the British Chemical Society (1972);
James Flack Norris Prize in Physical Organic
Chemistry from the American Chemical Socie-
ty (1980); Arthur C. Cope Award from the
American Chemical Society (1987) and
numerous other awards. Topic: “Geometric
Control of Binding and Catalysis.”

Steven C. Zimmerman, Ph.D. Columbia
University. NATO postdoctoral fellowship, Cam-
bridge University. Professor, University of II-
linois. Presidential Young Investigator Award,
National Science Foundation; Camille and
Henry Dreyfus Teacher-Scholar Award and Eli
Lilly Grantee. Topic: “Chemically Synthesized
Mimics of Biological Receptors and Enzyme
Catalysts.”

William C. DeGrado, Ph.D. The Univer-
sity of Chicago. Research Leader, E.I. du Pont
de Nemours & Co. Adjunct Professor of
Biophysics, Johns Hopkins Medical School.
Associate Editor, Proteins, Structure, Function,
Genetics. Editorial Board: Journal American
Chemical Society; Journal of Molecular
Recognition; International Journal of Peptide
and Protein Research; Protein Engineering.
Recipient: Du Vigneaud Award for Young In-
vestigators in Peptide Research; Protein Socie—
ty Young Investigator Award. Topic: “De Novo
Design of Helical Proteins.”

Andrew D. Hamilton, Ph.D. Cambridge
University. NATO postdoctoral fellowship,
Strasborg, France. Professor, University of Pitt—
sburgh. Visiting Professor of Chemistry, Univer-
sity of Kyoto ( 1987). Recipient of awards from
the Exxon Educational Foundation and Mobil.
Topic: “Molecular Recognition: New Artificial
Receptors for Complexation and Catalysis”.

Parking available free at Commonwealth Stadium on Cooper Drive. Shuttle buses run to the main campus. Additional parking
(for a fee) available in UK Medical Plaza Parking Garage, located approximately one block south of the Chemistry-Physics
Building; this garage can be accessed from both Rose and Limestone Streets—look for Medical Plaza Parking signs. For addi-
tional information, call John Richard, Department of Chemistry, (606) 257-1285.

Symposium supported by the Anna S. Naff Endowment Fund.