國立高雄大學圖資館 |

語系: 繁體中文

說明(常見問題)

圖資館首頁

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Understanding transglycosylase inhib...

LaTour, John Van Os.

Understanding transglycosylase inhibition: Chlorobiphenyl vancomycin and moenomycin A as targets for synthesis and modification.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Understanding transglycosylase inhibition: Chlorobiphenyl vancomycin and moenomycin A as targets for synthesis and modification.
作者:	LaTour, John Van Os.
面頁冊數:	145 p.
附註:	Adviser: Daniel Kahne.
附註:	Source: Dissertation Abstracts International, Volume: 65-08, Section: B, page: 4030.
Contained By:	Dissertation Abstracts International65-08B.
標題:	Chemistry, Organic.
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3143417
ISBN:	0496011669

Understanding transglycosylase inhibition: Chlorobiphenyl vancomycin and moenomycin A as targets for synthesis and modification.
LaTour, John Van Os.

Understanding transglycosylase inhibition: Chlorobiphenyl vancomycin and moenomycin A as targets for synthesis and modification. - 145 p.

Adviser: Daniel Kahne.

Thesis (Ph.D.)--Princeton University, 2004.

A model for transglycosylase inhibitors is presented, which requires both a transglycosylase binding portion and a localizing portion. Using this concept, a moenomycin-derived disaccharide transglycosylase inhibitor was attached to the vancomycin aglycone to make a novel hybrid inhibitor. The activity of this compound was dramatic, being roughly equivalent to chlorobiphenyl vancomycin itself against all strains tested (JACS 50, 12722).

ISBN: 0496011669Subjects--Topical Terms:

193634
Chemistry, Organic.

Understanding transglycosylase inhibition: Chlorobiphenyl vancomycin and moenomycin A as targets for synthesis and modification.
LDR:03511nmm _2200313 _450 001 162811
005 20051017073525.5
008 090528s2004 eng d
020 $a 0496011669
035 $a 00149312
040 $a UnM $c UnM
100 0 $a LaTour, John Van Os. $3 227956
245 1 0 $a Understanding transglycosylase inhibition: Chlorobiphenyl vancomycin and moenomycin A as targets for synthesis and modification.
300 $a 145 p.
500 $a Adviser: Daniel Kahne.
500 $a Source: Dissertation Abstracts International, Volume: 65-08, Section: B, page: 4030.
502 $a Thesis (Ph.D.)--Princeton University, 2004.
520 # $a A model for transglycosylase inhibitors is presented, which requires both a transglycosylase binding portion and a localizing portion. Using this concept, a moenomycin-derived disaccharide transglycosylase inhibitor was attached to the vancomycin aglycone to make a novel hybrid inhibitor. The activity of this compound was dramatic, being roughly equivalent to chlorobiphenyl vancomycin itself against all strains tested (JACS 50, 12722).
520 # $a In this thesis, the question of separating this second mechanism from the vancomycin aglycone is addressed. By tethering the chlorobiphenyl disaccharide to the aglycone through a two-carbon linker, we avoided the synthetic problem of directly glycosylating the aglycone. MIC data for a set of five compounds differing only in carbohydrate stereochemistry indicates that the chlorobiphenyl disaccharide participates in a unique and specific binding event ( Tetrahedron 58, 6585).
520 # $a Protection, degradation, and rephosphorylation of moenomycin A. As part of a total synthesis of the pentasaccharide antibiotic and transglycosylase inhibitor moenomycin A, we report the generation of a protected version of moenomycin A and cleavage of the anomeric phosphate to the intact pentasaccharide lactol. The generation of this compound represents the first non-enzymatic generation of the moenomycin pentasaccharide without phosphorus, and it should prove useful as a relay intermediate in the total synthesis and as a transglycosylase binding motif in the synthesis of moenomycin derivatives with better physical properties. It is further shown that the protected pentasaccharide lactol can be appropriately coupled and deprotected by attaching a free phosphate and a fluorescein-linked phosphate, confirming its usefulness for these purposes.
520 # $a Vancomycin derivatives. Vancomycin is a clinically important antibiotic that stops peptidoglycan synthesis by binding to the D-Ala-D-Ala portion of a peptidoglycan precursor. Resistance to vancomycin arose when certain enterococcal strains were able to change the terminal D-Ala in this substrate to D-lactate. A chlorobiphenyl derivative of vancomycin has shown a dramatic increase in activity against both sensitive and resistant strains. A few years ago, the Kahne group suggested an additional mechanism of action for this compound, involving enzyme binding and presented data indicating that D-Ala-D-Ala binding was not required for activity ( Science 284, 507).
590 $a School code: 0181.
650 # 0 $a Chemistry, Organic. $3 193634
650 # 0 $a Chemistry, Pharmaceutical. $3 206042
650 # 0 $a Chemistry, Biochemistry. $3 226900
690 $a 0487
690 $a 0490
690 $a 0491
710 0 # $a Princeton University. $3 212488
773 0 # $g 65-08B. $t Dissertation Abstracts International
790 $a 0181
790 1 0 $a Kahne, Daniel, $e advisor
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://libsw.nuk.edu.tw:81/login?url=http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3143417 $z http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3143417