1992
DOI: 10.1002/jps.2600810709
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Effect of Iontophoresis on In Vitro Skin Permeation of an Analogue of Growth Hormone Releasing Factor in the Hairless Guinea Pig Model

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Cited by 33 publications
(10 citation statements)
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“…Although there are reports of the iontophoretic enhancement of different peptide hormones with molecular weights (MW) in the 1-6 kDa range including luteinising hormone releasing hormone (4,5), calcitonin (6,7), growth hormone releasing hormone (8), human parathyroid hormone (9) and insulin (10,11), the effect of molecular size and protein structure on iontophoretic transport has not been well characterized. For a series of fluorescently-labeled poly-L-lysines (FITC-PLLs) ranging in MW from 4 to 26 kDa, iontophoresis enhanced the penetration of the 4 kDa analog but did not have any effect on the transport of the larger 26 kDa FITC-PLL (12).…”
Section: Introductionmentioning
confidence: 98%
“…Although there are reports of the iontophoretic enhancement of different peptide hormones with molecular weights (MW) in the 1-6 kDa range including luteinising hormone releasing hormone (4,5), calcitonin (6,7), growth hormone releasing hormone (8), human parathyroid hormone (9) and insulin (10,11), the effect of molecular size and protein structure on iontophoretic transport has not been well characterized. For a series of fluorescently-labeled poly-L-lysines (FITC-PLLs) ranging in MW from 4 to 26 kDa, iontophoresis enhanced the penetration of the 4 kDa analog but did not have any effect on the transport of the larger 26 kDa FITC-PLL (12).…”
Section: Introductionmentioning
confidence: 98%
“…[37 -39] For example, growth hormone releasing factor, a 3929-mw protein, was undetectable in the receptor fluid following application to HGP skin in both 1-chambered (static) and 2-chambered diffusion cells. [39] The enhanced penetration of Hev b 1, a 14.6-kD protein, as compared to Hev b 6.02, the smaller 4.7-kD protein, may be explained in part by its highly hydrophobic nature. [23] It has been proposed that Hev b 1 serves as a carrier protein by binding to large hydrophobic molecules thereby increasing their transport across cell membranes.…”
Section: Hev B 1 and Hev B 602 Dermal Penetration 301mentioning
confidence: 99%
“…The smaller, and therefore more mobile, buffer ions will carry more charge and be transported into the skin preferentially, reducing delivery efficiency. Increasing the buffer ion concentration of the donor solution, thereby increasing its ionic strength, or decreasing the concentration of solute, have been found to decrease the iontophoretic flux of both charged (Burnette and Marrero, 1986;Bellantone et al, 1986;Lelawongs et al, 1989;Green et al, 1991) and neutral (Burnette and Marrero, 1986;Burnette and Ongpipattanakul, 1987;Pikal and Shah, 1990a,b) solutes at relatively high concentraltions (0.05-0.5 M), while increasing flux at low concentrations (0.01-0.05 M) (Kumar et al, 1992). Removing buffer ions results in a steadily increasing delivery rate of peptide with time (Green et al, 1991).…”
Section: Aiche Journalmentioning
confidence: 99%