Force-dependent persistence length of DNA-intercalator complexes measured in single molecule stretching experiments

被引:22
|
作者
Bazoni, R. F. [1 ]
Lima, C. H. M. [1 ]
Ramos, E. B. [1 ]
Rocha, M. S. [1 ]
机构
[1] Univ Fed Vicosa, Dept Fis, Lab Fis Biol, Vicosa, MG, Brazil
关键词
HIGHER-ORDER STRUCTURE; OPTICAL TWEEZERS; ANTHRACYCLINE ANTIBIOTICS; MECHANICAL MEASUREMENTS; DEOXYRIBONUCLEIC-ACID; BIS-INTERCALATION; FLUORESCENCE DYE; BINDING; DRUG; MICROSCOPY;
D O I
10.1039/c5sm00706b
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
By using optical tweezers with an adjustable trap stiffness, we have performed systematic single molecule stretching experiments with two types of DNA-intercalator complexes, in order to investigate the effects of the maximum applied forces on the mechanical response of such complexes. We have explicitly shown that even in the low-force entropic regime the persistence length of the DNA-intercalator complexes is strongly force-dependent, although such behavior is not exhibited by bare DNA molecules. We discuss the possible physicochemical effects that can lead to such results. In particular, we propose that the stretching force can promote partial denaturation on the highly distorted double-helix of the DNA-intercalator complexes, which interfere strongly in the measured values of the persistence length.
引用
收藏
页码:4306 / 4314
页数:9
相关论文
共 47 条
  • [41] Native and fluorescent dye-dependent single-DNA molecule microchip dynamics as measured by differential interference contrast microscopy
    Oh, Doori
    Lee, Seungah
    Kang, Seong Ho
    CHEMICAL COMMUNICATIONS, 2011, 47 (32) : 9137 - 9139
  • [42] Single-Molecule Dynamics of the DNA-EcoRII Protein Complexes Revealed with High-Speed Atomic Force Microscopy
    Gilmore, Jamie L.
    Suzuki, Yuki
    Tamulaitis, Gintautas
    Siksnys, Virginijus
    Takeyasu, Kunio
    Lyubchenko, Yuri L.
    BIOCHEMISTRY, 2009, 48 (44) : 10492 - 10498
  • [43] Salt dependent binding of T4 gene 32 protein to single and double-stranded DNA:: Single molecule force spectroscopy measurements
    Pant, K
    Karpel, RL
    Rouzina, I
    Williams, MC
    JOURNAL OF MOLECULAR BIOLOGY, 2005, 349 (02) : 317 - 330
  • [44] Single molecule force spectroscopy of salt-dependent bacteriophage T7 gene 2.5 protein binding to single-stranded DNA
    Shokri, Leila
    Marintcheva, Boriana
    Richardson, Charles C.
    Rouzina, Ioulia
    Williams, Mark C.
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (50) : 38689 - 38696
  • [45] Salt dependent binding of T4 gene 32 protein to single- and double-stranded DNA: Single molecule force spectroscopy measurements
    Pant, K
    Karpel, RL
    Rouzina, I
    Williams, MC
    BIOPHYSICAL JOURNAL, 2005, 88 (01) : 351A - 351A
  • [46] Probing the Unbinding Kinetics of DNA-H-NS-DNA Protein Complexes by a High-Speed and High-Throughput Single-Molecule Pulling Assay using Atomic Force Microscopy
    Liang, Yan
    Baclayon, Marian
    van der Valk, Ramon
    Dame, Remus Th
    Roos, Wouter H.
    Wuite, Gijs J. L.
    BIOPHYSICAL JOURNAL, 2014, 106 (02) : 386A - 386A
  • [47] Length-Dependent, Single-Molecule Analysis of Short Double-Stranded DNA Fragments through Hydrogel-Filled Nanopores: A Potential Tool for Size Profiling Cell-Free DNA
    Al Sulaiman, Dana
    Gatehouse, Alfie
    Ivanov, Aleksandar P.
    Edel, Joshua B.
    Ladame, Sylvain
    ACS APPLIED MATERIALS & INTERFACES, 2021, 13 (23) : 26673 - 26681