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ASME Bacteriophage T4 Tail Fibers as a Basis for Structured Assemblies
100 стр.
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For the PDF eBook edition on The ASME Digital Collection, goto:
http://ebooks.asmedigitalcollection.asme.org/book.aspx?bookid=1350

By Paul Hyman and Timothy Harrah

Biomedical & Nanomedical Technologies (B&NT):Concise Monographs Series

Up to 40 volumes are planned for this concise monograph series,which focuses on the implementation of various engineeringprinciples in the conception, design, development, analysis andoperation of biomedical, biotechnological and nanotechnologysystems and applications.

Abstract: Bacteriophages, viruses that infectbacteria, have evolved a variety of complex protein structures tocarry their genomes between host cells. These proteins form thevirion particle which can be considered a mostly self-assembledprotein machine that protects the genome and effects genome entryinto new cells. Because bacteriophages (phages) are often found inharsh environments including animal digestive tracts, sewage, andsea water, virion particle proteins are typically very stable andresistant to changes in pH, salts, digestive proteases, and otheragents that typically denature or degrade proteins. BacteriophageT4 long tail fibers are specialized proteins that bind to the hostcell surface. They are very long (≈160 nm) and thin (≈3-5 nm) rigidfibrous multiprotein structures. The high length to width ratio ofthe long tail fibers (LTFs), rigidity, self-assembling propertiesplus chemical durability suggest that LTFs could be adapted into aself-patterning nanoscale protein structure or system. The longtail fibers of T4 are composed of 10 proteins, 3 copies each ofgene product (gp) 34, gp 36, and gp 37 plus a single copy of gp 35which forms the hinged "knee" of the tail fiber. Althoughcrystallizing whole tail fibers remains a challenge, otherstructural data on fiber fragments, related trimeric proteinfibers, and other data suggest that some type of repetitive betasecondary structure comprise the rigid rod portions of the tailfibers.

The presence of large segments of beta structure arising frommostly local interactions also support the proposition that tailfibers can withstand a variety of modifications withoutcompromising the overall structure and function of thebacteriophage. Toward the end of creating structured assemblies wehave constructed and tested a variety of tail fibers altered in gp37. These include deletions to alter the overall length andmodifications to a key segment where assembly is initiated toimprove assembly in vitro. We have developed an improvedpurification method for the assembled tail fiber. We have alsoadded a variety of attachment sites to several locations in the gp37 including a biotinylation site and an antibody binding epitope.These insertions do not appear to disrupt the gp 37 structure inany way and phages carrying these gp 37 modifications remainviable. In this monograph, we will review what is known about thestructure of the bacteriophage T4 tail fiber system and present amodel of how it can be adapted into a controlled self-assemblingsystem. We further review the published and unpublished work wehave completed on tail fiber purification andmodifications. 

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Hardcover