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Novel protein engineering approaches for chemoenzymatic synthesis of glycan polymers

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TitleInfo
Title
Novel protein engineering approaches for chemoenzymatic synthesis of glycan polymers
Name (type = personal)
NamePart (type = family)
Bandi
NamePart (type = given)
Chandra Kanth
NamePart (type = date)
1992
DisplayForm
Chandra Kanth Bandi
Role
RoleTerm (type = text); (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Chundawat
NamePart (type = given)
Shishir P.S.
DisplayForm
Shishir P.S. Chundawat
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Roth
NamePart (type = given)
Charles
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Charles Roth
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Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Zhang
NamePart (type = given)
Haoran
DisplayForm
Haoran Zhang
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Mayes
NamePart (type = given)
Heather
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Heather Mayes
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
outside member
Name (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (type = corporate)
NamePart
School of Graduate Studies
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
Genre (authority = ExL-Esploro)
ETD doctoral
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DateCreated (qualifier = exact); (encoding = w3cdtf); (keyDate = yes)
2021
DateOther (type = degree); (qualifier = exact); (encoding = w3cdtf)
2021-01
Language
LanguageTerm (authority = ISO 639-3:2007); (type = text)
English
Abstract
Glycans or carbohydrates are the most abundant class of biomolecules on the planet, but we are far from elucidating their role in the design and regulation of biological ecosystems spanning from organismal- to protein- level. Nearly every human cell-pathogen interaction and immune system related disorder or disease involves protein-glycan and glycan-glycan interactions at the molecular level. With the increase healthcare costs and greater emphasis by the pharmaceutical industry towards developing more effective biological drugs it becomes imperative to unravel the “glycan code”. Unfortunately, glycan synthesis is not template encoded and is the primary reason for the lack of efficient synthetic tools for widespread application. In nature, glycans are synthesized using membrane associated glycosyl transferases that are associated with several limitations including poor expression, solubility, and the need for expensive donor sugars for large scale synthesis. Alternatively, glycosyl hydrolases (GHs) can be reverse engineered and modulated to synthesize sugar polymers using their inherent transglycosylation property. However, transglycosylation pathway of GHs suffers from low yields because of enzyme’s natural preference towards competing water molecules leading to hydrolysis. Fortunately, protein engineering approaches such as rational engineering and directed evolution can address these challenges to shift the equilibrium towards transglycosylation. In this work, two protein engineering strategies that have been developed that can used engineer glycosyl hydrolysis for efficient glycan synthesis. The first approach is structure guided rational approach where a non-catalytic carbohydrate binding domain is fused to inactive GH family 5 enzymes to rescue the transglycosylation activity. The second approach is high throughput screening development to identify mutant variants that can synthesize glycan using azido-sugars. Here, an azide biosensing toolkit was developed that can be used for directed evolution based glycosynthase engineering. Both these engineering approaches can invariably be applied to many different glycosyl hydrolase families to generate potent transglycosidases.
Subject (authority = local)
Topic
Glycan synthesis
Subject (authority = RUETD)
Topic
Chemical and Biochemical Engineering
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
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ETD_11479
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application/pdf
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Extent
1 online resource (xx, 116 pages)
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references
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Title
School of Graduate Studies Electronic Theses and Dissertations
Identifier (type = local)
rucore10001600001
Location
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NjNbRU
Identifier (type = doi)
doi:10.7282/t3-ck1f-n868
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Rights

RightsDeclaration (ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder (type = personal)
Name
FamilyName
Bandi
GivenName
Chandra Kanth
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2021-01-18 17:03:08
AssociatedEntity
Name
Chandra Kanth Bandi
Role
Copyright holder
Affiliation
Rutgers University. School of Graduate Studies
AssociatedObject
Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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2021-01-19T16:37:15
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2021-01-19T16:37:21
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