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Kamat, Neha P

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Kamat

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Neha P

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Kamat, Neha P

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2015 - 20162

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Author's Publications: search.filters.isAuthorOfPublication.f55db823-c6ea-4f6a-a386-cdd2ce755160

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    Electrostatic Localization of RNA to Protocell Membranes by Cationic Hydrophobic Peptides
    (WILEY-VCH Verlag, 2015) Kamat, Neha P; Tobé, Sylvia; Hill, Ian; Szostak, Jack
    Cooperative interactions between RNA and vesicle membranes on the prebiotic earth may have led to the emergence of primitive cells. The membrane surface offers a potential platform for the catalysis of reactions involving RNA, but this scenario relies upon the existence of a simple mechanism by which RNA could become associated with protocell membranes. Here, we show that electrostatic interactions provided by short, basic, amphipathic peptides can be harnessed to drive RNA binding to both zwitterionic phospholipid and anionic fatty acid membranes. We show that the association of cationic molecules with phospholipid vesicles can enhance the local positive charge on a membrane and attract RNA polynucleotides. This phenomenon can be reproduced with amphipathic peptides as short as three amino acids. Finally, we show that peptides can cross bilayer membranes to localize encapsulated RNA. This mechanism of polynucleotide confinement could have been important for primitive cellular evolution.
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    Oligoarginine Peptides Slow Strand Annealing and Assist Nonenzymatic RNA Replication
    (2016) Jia, Tony Z.; Fahrenbach, Albert C.; Kamat, Neha P; Adamala, Katarzyna P.; Szostak, Jack
    The nonenzymatic replication of RNA is thought to have been a critical process required for the origin of life. One unsolved difficulty with nonenzymatic RNA replication is that template-directed copying of RNA results in a double-stranded product; following strand separation, rapid strand reannealing outcompetes slow nonenzymatic template copying, rendering multiple rounds of RNA replication impossible. Here we show that oligoarginine peptides slow the annealing of complementary oligoribonucleotides by up to several thousand-fold; however, short primers and activated monomers can still bind to template strands, and template-directed primer extension can still occur within a phase-separated condensed state, or coacervate. Furthermore, we show that within this phase, partial template copying occurs even in the presence of full-length complementary strands. This method for enabling further rounds of replication suggests one mechanism by which short, non-coded peptides could have enhanced early cellular fitness, potentially explaining how longer, coded peptides, i.e. proteins, came to prominence in modern biology.