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Revealing Fast Structural Dynamics in pH-Responsive Peptides with Time-Resolved X-ray Scattering.

ABSTRACT: Many biomaterials can adapt to changes in the local biological environment (such as pH, temperature, or ionic composition) in order to regulate function or deliver a payload. Such adaptation to environmental perturbation is typically a hierarchical process that begins with a response at a local structural level and then propagates to supramolecular and macromolecular scales. Understanding fast structural dynamics that occur upon perturbation is important for rational design of functional biomaterials. However, few nanosecond time-resolved methods can probe both intra- and intermolecular scales simultaneously with a high structural resolution. Here, we utilize time-resolved X-ray scattering to probe nanosecond to microsecond structural dynamics of poly-l-glutamic acid undergoing protonation via a pH jump initiated by photoexcitation of a photoacid. Our results provide insights into the protonation-induced hierarchical changes in packing of peptide chains, formation of a helical structure, and the associated collapse of the peptide chain.

SUBMITTER: Rimmerman D

PROVIDER: S-EPMC6533112 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature

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Revealing Fast Structural Dynamics in pH-Responsive Peptides with Time-Resolved X-ray Scattering.

Rimmerman Dolev D Leshchev Denis D Hsu Darren J DJ Hong Jiyun J Abraham Baxter B Henning Robert R Kosheleva Irina I Chen Lin X LX

The journal of physical chemistry. B 20190227 9

Many biomaterials can adapt to changes in the local biological environment (such as pH, temperature, or ionic composition) in order to regulate function or deliver a payload. Such adaptation to environmental perturbation is typically a hierarchical process that begins with a response at a local structural level and then propagates to supramolecular and macromolecular scales. Understanding fast structural dynamics that occur upon perturbation is important for rational design of functional biomate ...[more]

PMID: 30763085

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Project description:One of the most important questions in biological science is how a protein functions. When a protein performs its function, it undergoes regulated structural transitions. In this regard, to better understand the underlying principle of a protein function, it is desirable to monitor the dynamic evolution of the protein structure in real time. To probe fast and subtle motions of a protein in physiological conditions demands an experimental tool that is not only equipped with superb spatiotemporal resolution but also applicable to samples in solution phase. Time-resolved X-ray solution scattering (TRXSS), discussed in this Account, fits all of those requirements needed for probing the movements of proteins in aqueous solution. The technique utilizes a pump-probe scheme employing an optical pump pulse to initiate photoreactions of proteins and an X-ray probe pulse to monitor ensuing structural changes. The technical advances in ultrafast lasers and X-ray sources allow us to achieve superb temporal resolution down to femtoseconds. Because X-rays scatter off all atomic pairs in a protein, an X-ray scattering pattern provides information on the global structure of the protein with subangstrom spatial resolution. Importantly, TRXSS is readily applicable to aqueous solution samples of proteins with the aid of theoretical models and therefore is well suited for investigating structural dynamics of protein transitions in physiological conditions. In this Account, we demonstrate that TRXSS can be used to probe real-time structural dynamics of proteins in solution ranging from subtle helix movement to global conformational change. Specifically, we discuss the photoreactions of photoactive yellow protein (PYP) and homodimeric hemoglobin (HbI). For PYP, we revealed the kinetics of structural transitions among four transient intermediates comprising a photocycle and, by applying structural analysis based on ab initio shape reconstruction, showed that the signaling of PYP involves the protrusion of the N-terminus with significant increase of the overall protein size. For HbI, we elucidated the dynamics of complex allosteric transitions among transient intermediates. In particular, by applying structural refinement analysis based on rigid-body modeling, we found that the allosteric transition of HbI accompanies the rotation of quaternary structure and the contraction between two heme domains. By making use of the experimental and analysis methods presented in this Account, we envision that the TRXSS can be used to probe the structural dynamics of various proteins, allowing us to decipher the working mechanisms of their functions. Furthermore, when combined with femtosecond X-ray pulses generated from X-ray free electron lasers, TRXSS will gain access to ultrafast protein dynamics on sub-picosecond time scales.

Project description:Recent years have seen the development of new iron-centered N-heterocyclic carbene (NHC) complexes for solar energy applications. Compared to typical ligand systems, the NHC ligands provide Fe complexes with longer-lived metal-to-ligand charge transfer (MLCT) states. This increased lifetime is ascribed to strong ligand field splitting provided by the NHC ligands that raises the energy levels of the metal centered (MC) states and therefore reduces the deactivation efficiency of MLCT states. Among currently known NHC systems, [Fe(btbip)2]2+ (btbip = 2,6-bis(3-tert-butyl-imidazol-1-ylidene)pyridine) is a unique complex as it exhibits a short-lived MC state with a lifetime on the scale of a few hundreds of picoseconds. Hence, this complex allows for a detailed investigation, using 100 ps X-ray pulses from a synchrotron, of strong ligand field effects on the intermediate MC state in an NHC complex. Here, we use time-resolved wide angle X-ray scattering (TRWAXS) aided by density functional theory (DFT) to investigate the molecular structure, energetics and lifetime of the high-energy MC state in the Fe-NHC complex [Fe(btbip)2]2+ after excitation to the MLCT manifold. We identify it as a 260 ps metal-centered quintet (5MC) state, and we refine the molecular structure of the excited-state complex verifying the DFT results. Using information about the hydrodynamic state of the solvent, we also determine, for the first time, the energy of the 5MC state as 0.75 ± 0.15 eV. Our results demonstrate that due to the increased ligand field strength caused by NHC ligands, upon transition from the ground state to the 5MC state, the metal to ligand bonds extend by unusually large values: by 0.29 Å in the axial and 0.21 Å in the equatorial direction. These results imply that the transition in the photochemical properties from typical Fe complexes to novel NHC compounds is manifested not only in the destabilization of the MC states, but also in structural distortion of these states.

Dataset Information

Revealing Fast Structural Dynamics in pH-Responsive Peptides with Time-Resolved X-ray Scattering.

Publications

Revealing Fast Structural Dynamics in pH-Responsive Peptides with Time-Resolved X-ray Scattering.

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