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synthesis of novel amino acids with incorporation into peptides and synthesis of peptides with novel aggregation states (antibiotic, pore formation). [microform]
synthesis of novel amino acids with incorporation into peptides and synthesis of peptides with novel aggregation states (antibiotic, pore formation). [microform]
상세정보
- 자료유형
- 마이크로피시
- 청구기호
- 저자명
- 서명/저자
- synthesis of novel amino acids with incorporation into peptides and synthesis of peptides with novel aggregation states (antibiotic, pore formation). - [microform]
- 발행사항
- 형태사항
- 74 p. : microfiches ; 11×15 cm.
- 총서명
- UMI Dissertation
- 주기사항
- Source: Dissertation Abstracts International, Volume: 58-02, Section: B, page: 0700.
- 학위논문주기
- thesis (ph.d.)-- - the louisiana state university and agricultural and mechanical col., 1996.
- 초록/해제
- 요약Peptides exhibit properties based on the amino acids present in the peptide and structure the peptide assumes in its environment. For example, peptides have been shown to be antimicrobial when they are amphipathic and in an $\alpha$-helical shape. The mechanism for this antimicrobial activity is subject to dispute. One theory states that the peptides work by forming a "pore" through the cell membrane which causes a depolarization of the membrane and the cell lysis because of osmosis. Another theory states that the peptides merely compromise the integrity of the membrane by solubilizing the membrane.
- 초록/해제
- 요약In order for the "pore" theory of lytic activity to occur, the peptides must arrange themselves in a discrete aggregated fashion. The goal of this research is to explore the nature of the aggregated state of designed peptides through the use of CD spectroscopy and fluorescent labeling.
- 초록/해제
- 요약Several peptides were designed using a minimalist approach and were measured using CD spectroscopy to explore how the placement of leucines in the peptides cause a change in their propensity for aggregation. Using this information, the site for an incorporation of a fluorescently labeled peptide was chosen.
- 초록/해제
- 요약The synthesis of the fluorescently labeled amino acid presented an opportunity to explore different types of glycine templates and to find a quicker method for making the amino acid in high yields. After the synthesis of the amino acid, it was incorporated into the peptides and CD and fluorescence studies were accomplished. The result shows the peptides, when aggregated, align themselves in an antiparallel fashion.
- 복제주기
- Microfiche : UMI . microfiches;11×15 cm.
- 일반주제명
- 일반주제명
- 키워드
- 기타저자
- 기본자료저록
- Dissertation Abstracts International. 58-02B.
MARC
008970923s1996 us eng■001MOKWON00235092
■001AAV9720342
■00519981007131230
■008970923s1996 us eng
■035 ▼a(UnM)AAV9720342
■040 ▼aUnM▼cUnM▼dMOKWON
■090 ▼a540▼bC874s
■1001 ▼acowell, scott michael.
■24510▼asynthesis of novel amino acids with incorporation into peptides and synthesis of peptides with novel aggregation states (antibiotic, pore formation).▼h[microform]
■260 ▼aU.S.▼bthe louisiana state university and agricultural and mechanical col.▼c1996.
■300 ▼a74 p.▼bmicrofiches▼c11×15 cm.
■350 ▼a$50.6
■44000▼aUMI Dissertation
■500 ▼aSource: Dissertation Abstracts International, Volume: 58-02, Section: B, page: 0700.
■502 ▼athesis (ph.d.)--▼bthe louisiana state university and agricultural and mechanical col.▼d1996.
■520 ▼aPeptides exhibit properties based on the amino acids present in the peptide and structure the peptide assumes in its environment. For example, peptides have been shown to be antimicrobial when they are amphipathic and in an $\alpha$-helical shape. The mechanism for this antimicrobial activity is subject to dispute. One theory states that the peptides work by forming a "pore" through the cell membrane which causes a depolarization of the membrane and the cell lysis because of osmosis. Another theory states that the peptides merely compromise the integrity of the membrane by solubilizing the membrane.
■520 ▼aIn order for the "pore" theory of lytic activity to occur, the peptides must arrange themselves in a discrete aggregated fashion. The goal of this research is to explore the nature of the aggregated state of designed peptides through the use of CD spectroscopy and fluorescent labeling.
■520 ▼aSeveral peptides were designed using a minimalist approach and were measured using CD spectroscopy to explore how the placement of leucines in the peptides cause a change in their propensity for aggregation. Using this information, the site for an incorporation of a fluorescently labeled peptide was chosen.
■520 ▼aThe synthesis of the fluorescently labeled amino acid presented an opportunity to explore different types of glycine templates and to find a quicker method for making the amino acid in high yields. After the synthesis of the amino acid, it was incorporated into the peptides and CD and fluorescence studies were accomplished. The result shows the peptides, when aggregated, align themselves in an antiparallel fashion.
■533 ▼aMicrofiche▼cUMI▼emicrofiches;11×15 cm.
■590 ▼aSchool code: 0107.
■650 4▼aChemistry, Organic
■650 4▼aChemistry, Biochemistry
■653 ▼asynthesis▼aof▼anovel▼aamino▼aacids▼awith▼aincorporation▼ainto▼apeptides▼aand▼asynthesis▼aof▼apeptides▼awith▼anovel▼aaggregation▼astates▼a(antibiotic▼apore▼aformation).
■690 ▼a0490
■690 ▼a0487
■71020▼athe louisiana state university and agricultural and mechanical col..
■7730 ▼tDissertation Abstracts International▼g58-02B.
■790 ▼a0107
■791 ▼aPH.D.
■792 ▼a1996
