picture.gif (17583 bytes)
Porino Va


Ask Porino Va about the relevance of his research, and he will tell you this: “My project is unique because it concerns the use of organic chemistry in synthesizing potential drugs of the future.” Porino plans to continue his education in organic chemistry by attending graduate school, and eventually find his own niche working in industry. His talents aren’t limited; when not working in organic chemistry, Porino enjoys playing the guitar and bass. He’s also a fan of basketball, backpacking and snowboarding. triangle.gif (504 bytes)




Beta sheet interactions between proteins are crucial within the body. Beta peptide dimers may be able to cooperatively disrupt undesirable beta sheet interactions. We have synthesized a dityrosine-linked peptide dimer based on the B1 binding domain of Staphylococcal protein G (residues 17-21, LKGET). The monomers were prepared using Solid phase peptide synthesis, and dimerization was achieved through the use of horseradish peroxidase in a pH 9 borate buffer. The dimer was then characterized using HPLC, fluorescence and 1HNMR. This dimer may be able to disrupt the binding of protein G to the Fc domain of immunoglobulin G. This study is concerned with the synthesis and the investigation of secondary structural properties of the protein G dimer mimic [LY*GET]2, where Y* is a dityrosine crosslink. Initial ROESY data shows that the dimer adopts a structure in which the beta protons of tyrosine and the gamma protons of glutamic acid are near each other. Future research plans include scaling up to generate enough dimer for further 1HNMR studies and disruption assays. triangle.gif (504 bytes)

back.gif (221 bytes) next


Faculty Mentor                                                                                                                
facultypicture.gif (12811 bytes)

David Van Vranken

School of Physical

Porino is one of a new generation of chemists using organic synthesis to engineer models of biological interactions, atom by atom and bond by bond. Some proteins in the human body form carbon-carbon bonds between tyrosine sidechains. These dityrosine crosslinks exhibit great resiliency towards typical mechanisms of cleavage, either chemical or biological. In spite of their persistent nature, we know virtually nothing about how dityrosines affect local peptide structure or how we might use them to control the shapes and interactions of peptides. Porino’s motivation and persistence brought us closer to our long-term goals of understanding dityrosine crosslinks. The frontiers of science and technology continue to expand, but not beyond the reach of UCI’s undergraduates. The faculty mentoring system at UCI provides students like Porino with the opportunity to reach those frontiers in a relatively short period of time.triangle.gif (504 bytes)

back.gif (221 bytes)

If you wish to view the paper in its entirety, please select the link given to the PDF file.
pdf_logo.gif (126 bytes)
[Porino Va.pdf]

If you wish to download the Adobe Acrobat Reader,
please go to Adobe’s website (


Back to Journal 2001 Index


Copyright 2001 by the Regents of the University of California.  All rights reserved.