語系:
繁體中文
English
說明(常見問題)
圖資館首頁
登入
回首頁
切換:
標籤
|
MARC模式
|
ISBD
Studies toward design of an oligosaccharide scaffold to targetp53-MDM2.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Studies toward design of an oligosaccharide scaffold to targetp53-MDM2.
作者:
Sakurai, Kaori.
面頁冊數:
238 p.
附註:
Adviser: Dan Kahne.
附註:
Source: Dissertation Abstracts International, Volume: 64-01, Section: B, page: 0218.
Contained By:
Dissertation Abstracts International64-01B.
標題:
Chemistry, Organic.
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3078637
ISBN:
0493995137
Studies toward design of an oligosaccharide scaffold to targetp53-MDM2.
Sakurai, Kaori.
Studies toward design of an oligosaccharide scaffold to targetp53-MDM2.
[electronic resource] - 238 p.
Adviser: Dan Kahne.
Thesis (Ph.D.)--Princeton University, 2003.
A co-complex between MDM2 and an 8-residue p53 peptide analogue developed at Novartis is described. The 8 mer peptide binds MDM2 in short helical turns, similar to the wild type p53 peptide. Notably, the orientations of the key hydrophobic side chains were almost superimposable at the binding interface.
ISBN: 0493995137Subjects--Topical Terms:
193634
Chemistry, Organic.
Studies toward design of an oligosaccharide scaffold to targetp53-MDM2.
LDR
:02735nmm _2200289 _450
001
161846
005
20051017073343.5
008
230606s2003 eng d
020
$a
0493995137
035
$a
00148347
035
$a
161846
040
$a
UnM
$c
UnM
100
0
$a
Sakurai, Kaori.
$3
226925
245
1 0
$a
Studies toward design of an oligosaccharide scaffold to targetp53-MDM2.
$h
[electronic resource]
300
$a
238 p.
500
$a
Adviser: Dan Kahne.
500
$a
Source: Dissertation Abstracts International, Volume: 64-01, Section: B, page: 0218.
502
$a
Thesis (Ph.D.)--Princeton University, 2003.
520
#
$a
A co-complex between MDM2 and an 8-residue p53 peptide analogue developed at Novartis is described. The 8 mer peptide binds MDM2 in short helical turns, similar to the wild type p53 peptide. Notably, the orientations of the key hydrophobic side chains were almost superimposable at the binding interface.
520
#
$a
Overexpression of MDM2 inhibits p53 function and has been implicated in many human cancers. Molecules that target the p53-MDM2 interface are, therefore, anticipated to be therapeutic agents.
520
#
$a
To further explore if the peptide backbone can be replaced by a preorganized, non-peptidic scaffold to achieve the required side chain presentation for the binding, oligosaccharide scaffold was designed. A synthetic route for the functionalized oligosaccharide scaffold was developed using the sulfoxide glycosylation reaction as a key coupling method. The functionalized oligosaccharide scaffold aggregated, making it difficult to evaluate their MDM2 binding activity. However, a modular and convergent synthesis of functionalized oligosaccharides may potentially be utilized to target other protein-protein interfaces that involve similar helical recognition motifs as in the p53-MDM2 interaction.
520
#
$a
Two approaches toward the design of small molecule scaffolds that target p53-MDM2 are presented. In one, we probed the role of the peptide backbone of the p53 peptide in MDM2 binding, using a retro and a retroinverso peptide. The conformational behavior and the activity of these backbone modified peptides are described. We found that specific side chain presentation is important for binding but the peptide backbone structure is not. Our results demonstrate the utility of retroinverso peptides for probing the nature of peptide-protein interactions.
590
$a
School code: 0181.
650
# 0
$a
Chemistry, Organic.
$3
193634
710
0 #
$a
Princeton University.
$3
212488
773
0 #
$g
64-01B.
$t
Dissertation Abstracts International
790
$a
0181
790
1 0
$a
Kahne, Dan,
$e
advisor
791
$a
Ph.D.
792
$a
2003
856
4 0
$u
http://libsw.nuk.edu.tw/login?url=http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3078637
$z
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3078637
筆 0 讀者評論
全部
電子館藏
館藏
1 筆 • 頁數 1 •
1
條碼號
館藏地
館藏流通類別
資料類型
索書號
使用類型
借閱狀態
預約狀態
備註欄
附件
000000000339
電子館藏
1圖書
學位論文
一般使用(Normal)
在架
0
1 筆 • 頁數 1 •
1
多媒體
多媒體檔案
http://libsw.nuk.edu.tw/login?url=http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3078637
評論
新增評論
分享你的心得
Export
取書館別
處理中
...
變更密碼
登入