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Synthesis and Biological Evaluation of (Hydroxethyl) Urea Peptidomimetic Transition-State Analogs for Use in a Click Che...

Permanent Link: http://ncf.sobek.ufl.edu/NCFE004097/00001

Material Information

Title: Synthesis and Biological Evaluation of (Hydroxethyl) Urea Peptidomimetic Transition-State Analogs for Use in a Click Chemistry Approach to Studying the Gamma-Secretase Complex
Physical Description: Book
Language: English
Creator: Gars, Eric
Publisher: New College of Florida
Place of Publication: Sarasota, Fla.
Creation Date: 2009
Publication Date: 2009

Subjects

Subjects / Keywords: Synthesis
Alzheimer's Disease
Click Chemistry
Genre: bibliography   ( marcgt )
theses   ( marcgt )
government publication (state, provincial, terriorial, dependent)   ( marcgt )
born-digital   ( sobekcm )
Electronic Thesis or Dissertation

Notes

Abstract: Alzheimer's disease (AD) is an incurable, neurodegenerative, and terminal illness affecting nearly 30 million people worldwide. The disease is characterized by the accumulation of fibrous tangles in the brain called amyloid plaques. These fibrillar amyloid plaques aggregate around neurons and blood vessels and restrict blood flow, leading to tissue atrophy and ultimately death. While the cause of AD is not completely understood, strong evidence implicates a 42 amino acid splicing variant of the beta-amyloid precursor protein (APP), Abeta42, as the nucleating factor in the development of plaques. The final cleavage site of APP is a multi-subunit, transmembrane enzyme, the gamma-secretase complex. Elucidation of the gammasecretase complex structure is complicated by its location in the plasma membrane, which prevents crystallographic methods of structure determination. The use of active-site directed affinity probes, though, has been effective in isolation and characterization of the enzyme complex. This thesis details the synthesis and biological evaluation of a series of peptidomimetic transition-state analogs containing Cterminal azide and alkyne functional groups for subsequent use in a Click Chemistry approach to studying the Alzheimer's disease (AD) is an incurable, neurodegenerative, and terminal illness affecting nearly 30 million people worldwide. The disease is characterized by the accumulation of fibrous tangles in the brain called amyloid plaques. These fibrillar amyloid plaques aggregate around neurons and blood vessels and restrict blood flow, leading to tissue atrophy and ultimately death. While the cause of AD is not completely understood, strong evidence implicates a 42 amino acid splicing variant of the beta-amyloid precursor protein (APP), Abeta42, as the nucleating factor in the development of plaques. The final cleavage site of APP is a multi-subunit, transmembrane enzyme, the gamma-secretase complex. Elucidation of the gammasecretase complex structure is complicated by its location in the plasma membrane, which prevents crystallographic methods of structure determination. The use of active-site directed affinity probes, though, has been effective in isolation and characterization of the enzyme complex. This thesis details the synthesis and biological evaluation of a series of peptidomimetic transition-state analogs containing Cterminal azide and alkyne functional groups for subsequent use in a Click Chemistry approach to studying the gamma-secretase complex.
Statement of Responsibility: by Eric Gars
Thesis: Thesis (B.A.) -- New College of Florida, 2009
General Note: Online version not currently available.
Electronic Access: RESTRICTED TO NCF STUDENTS, STAFF, FACULTY, AND ON-CAMPUS USE
Bibliography: Includes bibliographical references.
Source of Description: This bibliographic record is available under the Creative Commons CC0 public domain dedication. The New College of Florida, as creator of this bibliographic record, has waived all rights to it worldwide under copyright law, including all related and neighboring rights, to the extent allowed by law.
Local: Faculty Sponsor: Scudder, Paul

Record Information

Source Institution: New College of Florida
Holding Location: New College of Florida
Rights Management: Applicable rights reserved.
Classification: local - S.T. 2009 G2
System ID: NCFE004097:00001

Permanent Link: http://ncf.sobek.ufl.edu/NCFE004097/00001

Material Information

Title: Synthesis and Biological Evaluation of (Hydroxethyl) Urea Peptidomimetic Transition-State Analogs for Use in a Click Chemistry Approach to Studying the Gamma-Secretase Complex
Physical Description: Book
Language: English
Creator: Gars, Eric
Publisher: New College of Florida
Place of Publication: Sarasota, Fla.
Creation Date: 2009
Publication Date: 2009

Subjects

Subjects / Keywords: Synthesis
Alzheimer's Disease
Click Chemistry
Genre: bibliography   ( marcgt )
theses   ( marcgt )
government publication (state, provincial, terriorial, dependent)   ( marcgt )
born-digital   ( sobekcm )
Electronic Thesis or Dissertation

Notes

Abstract: Alzheimer's disease (AD) is an incurable, neurodegenerative, and terminal illness affecting nearly 30 million people worldwide. The disease is characterized by the accumulation of fibrous tangles in the brain called amyloid plaques. These fibrillar amyloid plaques aggregate around neurons and blood vessels and restrict blood flow, leading to tissue atrophy and ultimately death. While the cause of AD is not completely understood, strong evidence implicates a 42 amino acid splicing variant of the beta-amyloid precursor protein (APP), Abeta42, as the nucleating factor in the development of plaques. The final cleavage site of APP is a multi-subunit, transmembrane enzyme, the gamma-secretase complex. Elucidation of the gammasecretase complex structure is complicated by its location in the plasma membrane, which prevents crystallographic methods of structure determination. The use of active-site directed affinity probes, though, has been effective in isolation and characterization of the enzyme complex. This thesis details the synthesis and biological evaluation of a series of peptidomimetic transition-state analogs containing Cterminal azide and alkyne functional groups for subsequent use in a Click Chemistry approach to studying the Alzheimer's disease (AD) is an incurable, neurodegenerative, and terminal illness affecting nearly 30 million people worldwide. The disease is characterized by the accumulation of fibrous tangles in the brain called amyloid plaques. These fibrillar amyloid plaques aggregate around neurons and blood vessels and restrict blood flow, leading to tissue atrophy and ultimately death. While the cause of AD is not completely understood, strong evidence implicates a 42 amino acid splicing variant of the beta-amyloid precursor protein (APP), Abeta42, as the nucleating factor in the development of plaques. The final cleavage site of APP is a multi-subunit, transmembrane enzyme, the gamma-secretase complex. Elucidation of the gammasecretase complex structure is complicated by its location in the plasma membrane, which prevents crystallographic methods of structure determination. The use of active-site directed affinity probes, though, has been effective in isolation and characterization of the enzyme complex. This thesis details the synthesis and biological evaluation of a series of peptidomimetic transition-state analogs containing Cterminal azide and alkyne functional groups for subsequent use in a Click Chemistry approach to studying the gamma-secretase complex.
Statement of Responsibility: by Eric Gars
Thesis: Thesis (B.A.) -- New College of Florida, 2009
General Note: Online version not currently available.
Electronic Access: RESTRICTED TO NCF STUDENTS, STAFF, FACULTY, AND ON-CAMPUS USE
Bibliography: Includes bibliographical references.
Source of Description: This bibliographic record is available under the Creative Commons CC0 public domain dedication. The New College of Florida, as creator of this bibliographic record, has waived all rights to it worldwide under copyright law, including all related and neighboring rights, to the extent allowed by law.
Local: Faculty Sponsor: Scudder, Paul

Record Information

Source Institution: New College of Florida
Holding Location: New College of Florida
Rights Management: Applicable rights reserved.
Classification: local - S.T. 2009 G2
System ID: NCFE004097:00001

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