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. Author manuscript; available in PMC: 2021 May 1.
Published in final edited form as: Small. 2020 Jan 27;16(21):e1906674. doi: 10.1002/smll.201906674

Figure 3. DMD simulations of a bPEI-capped AgNC interacting with a FapC monomer and a FapC fragment dimer.

Figure 3.

(A-C) Full-length FapC monomer (R1L1R2L2R3) with and without the presence of the bPEI-capped AgNC. (A) Overall secondary structure contents of the full-length FapC monomer. (B) The bPEI-capped AgNC-binding probability, and the β-sheet and α-helix propensities of each residue. (C) Three representative structures of FapC in the absence (upper) and presence (lower) of the AgNC. The peptide shown as cartoon is colored rainbow from blue (N-terminus) to red (C-terminus). The core of the AgNC is shown as spheres and bPEIs as sticks. (D-E) A L1R2 dimer with and without the presence of the bPEI-capped AgNC. (D) Overall secondary structure contents of the dimer. (E) The binding probability with bPEI-capped AgNC or AgNP, and the β-sheet and α-helix propensities of each residue. (F) Representative structures of the L1R2 dimer in the absence (upper) and presence of the bPEI-capped AgNC (lower left) and AgNP (lower right). The two peptides are colored differently.