Proteolytic Activity at Quantum Dot-Conjugates: Kinetic Analysis Reveals Enhanced Enzyme Activity and Localized Interfacial "Hopping"

被引：115

作者：

Algar, W. Russ ^{[1
,3
]}

Malonoski, Anthony ^{[1
]}

Deschamps, Jeffrey R. ^{[1
]}

Banco-Canosa, Juan B. ^{[4
,5
]}

Susumu, Kimihiro ^{[2
]}

Stewart, Michael H. ^{[2
]}

Johnson, Brandy J. ^{[1
]}

Dawson, Philip E. ^{[4
,5
]}

Medintz, Igor L. ^{[1
]}

机构：

[1] USN, Ctr Bio Mol Sci & Engn, Res Lab, Washington, DC 20375 USA

[2] USN, Div Opt Sci, Res Lab, Washington, DC 20375 USA

[3] George Mason Univ, Coll Sci, Fairfax, VA 22030 USA

[4] Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA

[5] Scripps Res Inst, Dept Chem, La Jolla, CA 92037 USA

来源：

NANO LETTERS | 2012年 / 12卷 / 07期

基金：

加拿大自然科学与工程研究理事会;

关键词：

Quantum dot; nanoparticle; peptide; proteolysis; kinetics; FRET; RESONANCE ENERGY-TRANSFER; BIOCOMPATIBLE SEMICONDUCTOR; QUANTITATIVE-ANALYSIS; GOLD NANOPARTICLES; STABILITY; LIGANDS; CHYMOTRYPSIN; PARAMETERS; INHIBITORS; CATALYSIS;

D O I：

10.1021/nl301727k

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Recent studies show that polyvalent, ligand-modified nanoparticles provide significantly enhanced binding characteristics compared to isolated ligands. Here, we assess the ability of substrate-modified nanoparticles to provide enhanced enzymatic activity. Energy transfer assays allowed quantitative, real-time measurement of proteolytic digestion at polyvalent quantum dot-peptide conjugates. Enzymatic progress curves were analyzed using an integrated Michaelis Menten (MM) formalism, revealing mechanistic details, including deviations from classic MM-behavior. A "hopping" mode of proteolysis at the nanoparticle was identified, confirming enhanced activity.

引用

页码：3793 / 3802

页数：10

共 6 条

[1] Proteolytic activity monitored by fluorescence resonance energy transfer through quantum-dot–peptide conjugates
Igor L. Medintz
Aaron R. Clapp
Florence M. Brunel
Theresa Tiefenbrunn
H. Tetsuo Uyeda
Eddie L. Chang
Jeffrey R. Deschamps
Philip E. Dawson
Hedi Mattoussi
Nature Materials, 2006, 5 : 581 - 589
[2] Proteolytic activity monitored by fluorescence resonance energy transfer through quantum-dot-peptide conjugates
Medintz, Igor L.
Clapp, Aaron R.
Brunel, Florence M.
Tiefenbrunn, Theresa
Uyeda, H. Tetsuo
Chang, Eddie L.
Deschamps, Jeffrey R.
Dawson, Philip E.
Mattoussi, Hedi
NATURE MATERIALS, 2006, 5 (07) : 581 - 589
[3] Multiplex Sensing of Protease and Kinase Enzyme Activity via Orthogonal Coupling of Quantum Dot Peptide Conjugates
Lowe, Stuart B.
Dick, John A. G.
Cohen, Bruce E.
Stevens, Molly M.
ACS NANO, 2012, 6 (01) : 851 - 857
[4] Quantum Dot-Peptide Conjugates as Energy Transfer Probes for Sensing the Proteolytic Activity of Matrix Metalloproteinase-14
Jin, Zhicheng
Dridi, Narjes
Palui, Goutam
Palomo, Valle
Jokerst, Jesse V.
Dawson, Phillip E.
Sang, Qing-Xiang Amy
Mattoussi, Hedi
ANALYTICAL CHEMISTRY, 2023, 95 (05) : 2713 - 2722
[5] Quantum dot based enzyme activity sensors present deviations from Michaelis-Menten kinetic model
Diaz, Sebastian A.
Brown, Carl W., III
Malanoski, Anthony P.
Oh, Eunkeu
Susumu, Kimihiro
Medintz, Igor L.
COLLOIDAL NANOPARTICLES FOR BIOMEDICAL APPLICATIONS XI, 2016, 9722
[6] Kinetic Analysis of Human PrimPol DNA Polymerase Activity Reveals a Generally Error-Prone Enzyme Capable of Accurately Bypassing 7,8-Dihydro-8-oxo-2′-deoxyguanosine
Zafar, Maroof K.
Ketkar, Amit
Lodeiro, Maria F.
Cameron, Craig E.
Eoff, Robert L.
BIOCHEMISTRY, 2014, 53 (41) : 6584 - 6594

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