Fluorophore-Labeled <i>S</i>-Nitrosothiols

Chen, Xi; Zhang, Wen; Xian, Ming; Wang, Kai; Ramachandran, Niroshan; Tang, Xiaoping; Schlegel, H. Bernhard; Mutus, Bülent; Wang, P. G.

doi:10.1021/jo015658p

Cited by 25 publications

(18 citation statements)

References 44 publications

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“…Both experiments and quantum chemistry calculations (27) are in agreement that the interaction between RSNO and aromatic amino acids may contribute to the observed GSNO-fibrinogen interactions. RSNO-dependent allosteric interactions are predicted to occur in regions of the ␣C chains that are rich in aromatic residues, converting them to more ordered ␣-helices.…”

Section: Discussionsupporting

confidence: 73%

“…The quenching was attributed to energy transfer between the dansyl moiety donor (excitation 340 nm; emission 540 nm) and RS-NO (acceptor, absorbance 543 nm), and, in order for this process to occur, the RS-NO must ''lay over'' the dansyl ring. Recent calculations by Chen et al (27) indicated that the interaction between the SNO moiety and the dansyl ring is energetically favorable.…”

Section: Discussionmentioning

confidence: 99%

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Evidence for S -nitrosothiol-dependent changes in fibrinogen that do not involve transnitrosation or thiolation

Akhter

Vignini

Zhang

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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S-nitrosoglutathione (GSNO, 50 M) inhibited the initial rate of thrombin-catalyzed human and bovine fibrinogen polymerization by Ϸ50% to 68% respectively. Inhibition was also observed with other structurally varied S-nitrosothiols (RSNOs) including sugar derivatives of S-nitroso-N-acetylpenicillamine (SNAP). The fact that the same concentration of GSNO had no effect on thrombindependent hydrolysis of tosylglycylprolylarginine-4-nitroanilide acetate suggested that this inhibition was due to GSNO-induced changes in fibrinogen structure. This result was confirmed by CD spectroscopy where GSNO or S-nitrosohomocysteine increased the ␣-helical content of fibrinogen by Ϸ15% and 11%, respectively. S-carboxymethylamido derivatives of glutathione or homocysteine had no effect on the fibrinogen secondary structure. The GSNO-dependent secondary structural effects were reversed on gel filtration chromatography, suggesting that the effects were allosteric. Further evidence for fibrinogen-GSNO interactions was obtained from GSNO-dependent quenching of the intrinsic fibrinogen Trp fluorescence and the perturbation of the GSNO circular dichroic absorbance as a function of [fibrinogen]. The K ds of 3 to 10 M for fibrinogen-GSNO interactions with a stoichiometry of 2:1 (GSNO:fibrinogen) were estimated from isothermal titration calorimetry and fluorescence quenching, respectively. These results suggest that RSNOs induce changes to fibrinogen structure by interacting at specific aromatic rich domains. Three such putative RSNO-binding domains have been identified in the unordered, aromatic residue-rich C-termini of the ␣-chains of fibrinogen.

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Section: Discussionsupporting

confidence: 73%

Section: Discussionmentioning

confidence: 99%

Evidence for S -nitrosothiol-dependent changes in fibrinogen that do not involve transnitrosation or thiolation

Akhter

Vignini

Zhang

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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“…This method obviously does not extend to the probes bearing multiple decomposition pathways, e.g., fluorophore-labeled nitrosothiols. 52,53 We tested the feasibility of our NO donors for two-photon triggered release of NO and for two-photon imaging, also with NOD545f as an example. First, the RAW264.7 cells were incubated with NOD545f (5 μM) for 15 min and were imaged upon excitation by a two-photon laser at 800 nm.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Photocalibrated NO Release from N-Nitrosated Napthalimides upon One-Photon or Two-Photon Irradiation

Zhang¹,

Wu²,

Shang³

et al. 2016

Anal. Chem.

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NO donors are routinely used as the exogenous source in in vitro studies. However, the kinetics or the dose of NO release from the existing donors is not readily monitored. This complicates the elucidation of the involvement of NO in a biological response. We report herein a series of NO donors (NOD545a-g), whose NO release is triggered by UV light at 365 nm or a two-photon laser at 740 nm, and importantly, their NO release is accompanied by a drastic fluorescence turn-on, which has been harnessed to follow the kinetics and dose of NO release in a real-time fashion with spectroscopic methods or microscopic methods in in vitro studies. These merits have rendered NOD545a-g useful molecular tools in NO biology.

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“…The commercial compound N-acetylhomocysteine thiolactone, also referred to as citiolone, has been used for the transformation of ε-NH 2 groups of lysine residues in proteins [228,229] and the thiolation of a large variety of biological macromolecular systems has already been reported [230][231][232]. The first description of this method in peptide derivatization dates back to 1956, but it is only recently that our and later other research groups extended thiolactone chemistry to the synthesis of functional polymer materials [233].…”

Section: Thiolactonesmentioning

confidence: 99%