Fluorescent dyes alter intracellular targeting and function of cell-penetrating tetrapeptides Hazel H. Szeto * ,1 , Peter W. Schiller † , Kesheng Zhao * and Guoxiong Luo * * Department of Pharmacology, Joan and Sanford I. Weill Medical College of Cornell University, New York, New York, USA; and † Laboratory of Chemical Biology and Peptide Research, Clinical Research Institute of Montreal, Montreal, Quebec, Canada 1 Correspondence: Department of Pharmacology, Weill Medical College of Cornell University, 1300 York Ave., New York, NY 10021, USA. Email: hhszeto@med.cornell.edu <h3>SPECIFIC AIMS</h3> Fluorescent labels are commonly used to investigate the mechanisms of cellular uptake and intracellular distribution of cell-penetrating peptides. However, labels such as fluorescein and rhodamine are relatively large and very lipophilic, and may significantly alter physicochemical properties of small peptides. To minimize the impact of the fluorescent probe on a tetrapeptide, we substituted one of the amino acids (Lys 4 ) in a tetrapeptide ([Dmt 1 ]DALDA, Dmt-D-Arg-Phe-Lys-NH 2 where Dmt=2',6'-dimethyltyrosine) with two different fluorescent amino acids (ß-dansyl-L-α,ß-diaminopropionic acid (dnsDap 4 ) or ß-anthraniloyl-L-α,ß-diaminopropionic acid (atnDap 4 ). Initial studies with confocal laser scanning microscopy (CLSM) showed very different localization patterns for the two fluorescent analogs, with [Dmt 1 ,atnDap 4
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Fluorescent dyes alter intracellular targeting and function of cell-penetrating tetrapeptides
Szeto, Hazel H.; Schiller, Peter W.; Zhao, Kesheng; Luo, Guoxiong
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, Volume 19 (1): 118
Fed of American Socs for Experimental Biology – Jan 1, 2005
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