Abstract
Maurocalcine (MCa) is the first natural cell penetrating peptide to be discovered in animal venom. In addition to the fact that it represents a potent vector for the cell penetration of structurally diverse therapeutic compounds, MCa also displays several distinguishing features that make it a potential peptide of choice for clinical and biotechnological applications. The aim of the present study was to gain new information about the properties of MCa in vivo in order to delineate the future potential applications of this vector. For this purpose, two analogues of this peptide with (Tyr-MCa) and without (Lin-Tyr-MCa) disulfide bridges were synthesized, radiolabeled with 125I, and their in vitro stabilities were first evaluated in mouse blood. The results indicated that 125I-Tyr-MCa was stable in vitro and that the disulfide bridges conferred a competitive advantage for the stability of peptide. Following in vivo injection in mice, 125I-Tyr-MCa targeted peripheral organs with interesting quantitative differences and the main route of peptide elimination was renal.
Highlights
Maurocalcine (MCa) has been extracted from the venom of the Scorpio maurus palmatus and identified as a 33-mer peptide [1]
While MCa is recognized as a competitive cell penetrating peptides (CPP) due to its low concentration efficacy and ability to reach the cytoplasm, additional efforts were made to obtain MCa analogues deprived of undesirable pharmacological effects yet with preserved cell penetration properties
Venomous toxins are delivered in vivo and are tailored to survive enough time within the blood stream of animal preys until the pharmacological potential of these molecules has been fully exploited. Two analogues of this peptide were synthesized in order to investigate the in vivo properties of MCa, namely Tyr-MCa that like the natural form of MCa contains three disulfide bridges according to the pattern of Cys3–Cys17, Cys10–Cys21 and Cys16–Cys32, and Lin-Tyr-MCa without disulfide bridges lacking any three-dimensional structure [8]
Summary
Maurocalcine (MCa) has been extracted from the venom of the Scorpio maurus palmatus and identified as a 33-mer peptide [1]. Considering the potential of the natural form of MCa as a vector, we quantitatively investigated its cell penetration properties in a recent study This was done by grafting an additional Tyr residue at the N-terminus of the peptide followed by appropriate iodination with 125I to provide first Tyr-MCa and 125I-Tyr-MCa. The results indicated that dose-dependent accumulation of radioiodinated Tyr-MCa was observed in the nucleus and cytoplasm of rat F98 glioma cells with >24 h cellular retention [13]. Venomous toxins are delivered in vivo and are tailored to survive enough time within the blood stream of animal preys until the pharmacological potential of these molecules has been fully exploited Two analogues of this peptide were synthesized in order to investigate the in vivo properties of MCa, namely Tyr-MCa that like the natural form of MCa contains three disulfide bridges according to the pattern of Cys3–Cys, Cys10–Cys and Cys16–Cys, and Lin-Tyr-MCa without disulfide bridges lacking any three-dimensional structure [8]. The present study will help to delineate the in vivo potential of MCa as a CPP
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