Robert G. Alberstein

University of California, San Diego

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F. Akif Tezcan

University of California, San Diego

Richard Grey

National Institutes of Health

Shuai Zhang

Zhengzhou University of Light Industry

Mark L. Mayer

National Institutes of Health

Austin Zimmet

University of Pennsylvania

Jake Bailey

University of California, San Diego

Deborah E. Hunka

Leidos (United States)

David V. Hansen

Brigham Young University

Heidi Ackerly Wallweber

Genentech

Albert Y. Lau

Johns Hopkins Medicine

Cooperative Institutions

University of California, San Diego

University of Washington

Seattle University

Genentech

Pacific Northwest National Laboratory

University of California System

Physical Sciences (United States)

University of California, San Francisco

University of Chicago

Environmental Molecular Sciences Laboratory

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Rapid affinity optimization of an anti-TREM2 clinical lead antibody by cross-lineage immune repertoire mining

Nature Communications (2024)

Yi-Chun Hsiao Heidi Ackerly Wallweber Robert G. Alberstein Zhonghua Lin Changchun Du

Lineage (genetic)

Lead (geology)

10.1038/s41467-024-52442-y

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Citations (1)

Assembly of a patchy protein into variable 2D lattices via tunable multiscale interactions

Nature Communications (2020)

Shuai Zhang Robert G. Alberstein James J. De Yoreo F. Akif Tezcan

Self-assembly of molecular building blocks into higher-order structures is exploited in living systems to create functional complexity and represents a powerful strategy for constructing new materials. As nanoscale building blocks, proteins offer unique advantages, including monodispersity and atomically tunable interactions. Yet, control of protein self-assembly has been limited compared to inorganic or polymeric nanoparticles, which lack such attributes. Here, we report modular self-assembly of an engineered protein into four physicochemically distinct, precisely patterned 2D crystals via control of four classes of interactions spanning Ångström to several-nanometer length scales. We relate the resulting structures to the underlying free-energy landscape by combining in-situ atomic force microscopy observations of assembly with thermodynamic analyses of protein-protein and -surface interactions. Our results demonstrate rich phase behavior obtainable from a single, highly patchy protein when interactions acting over multiple length scales are exploited and predict unusual bulk-scale properties for protein-based materials that ensue from such control.

10.1038/s41467-020-17562-1

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Citations (44)

Constructing protein polyhedra via orthogonal chemical interactions

Nature (2020)

Eyal Golub Rohit H. Subramanian Julian Esselborn Robert G. Alberstein Jake Bailey

Polyhedron

Stoichiometry

10.1038/s41586-019-1928-2

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Citations (118)

Glycine activated ion channel subunits encoded by ctenophore glutamate receptor genes

Proceedings of the National Academy of Sciences (2015)

Robert G. Alberstein Richard Grey Austin Zimmet David K. Simmons Mark L. Mayer

Significance We report the characterization of two novel glutamate receptor subunits from recently sequenced ctenophore genomes. The origin of vertebrate NMDA subtype ionotropic glutamate receptors (iGluRs), which play a major role in synaptic plasticity and which require both glutamate and glycine for activation of ion channel gating, is not well understood. Using X-ray crystallography of the ligand binding domains of iGluRs from the comb jelly Mnemiopsis leidyi and the sea gooseberry Pleurobrachia bachei , candidates for the earliest lineage metazoans, we discovered that a large subset of these iGluR subunits form glycine receptors. Similarities to modern-day NMDA receptors suggest NMDA and ctenophore receptors may provide clues to the role of iGluRs in the evolution of neural systems in metazoa.

Kainate receptor

Ionotropic glutamate receptor

Conserved sequence

10.1073/pnas.1513771112

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Citations (52)

Ion-dependent protein–surface interactions from intrinsic solvent response

Proceedings of the National Academy of Sciences (2021)

Jesse L. Prelesnik Robert G. Alberstein Shuai Zhang Harley Pyles David Baker

The phyllosilicate mineral muscovite mica is widely used as a surface template for the patterning of macromolecules, yet a molecular understanding of its surface chemistry under varying solution conditions, required to predict and control the self-assembly of adsorbed species, is lacking. We utilize all-atom molecular dynamics simulations in conjunction with an electrostatic analysis based in local molecular field theory that affords a clean separation of long-range and short-range electrostatics. Using water polarization response as a measure of the electric fields that arise from patterned, surface-bound ions that direct the adsorption of charged macromolecules, we apply a Landau theory of forces induced by asymmetrically polarized surfaces to compute protein-surface interactions for two muscovite-binding proteins (DHR10-mica6 and C98RhuA). Comparison of the pressure between surface and protein in high-concentration KCl and NaCl aqueous solutions reveals ion-specific differences in far-field protein-surface interactions, neatly capturing the ability of ions to modulate the surface charge of muscovite that in turn selectively attracts one binding face of each protein over all others.

Muscovite

Electrostatics

Static electricity

Surface charge

Protein Adsorption

Surface forces apparatus

10.1073/pnas.2025121118

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Citations (15)

Designed 2D protein crystals as dynamic molecular gatekeepers for a solid-state device

Nature Communications (2024)

Sanahan Vijayakumar Robert G. Alberstein Zhi-Yin Zhang Yi‐Sheng Lu Adriano Chan

Abstract The sensitivity and responsiveness of living cells to environmental changes are enabled by dynamic protein structures, inspiring efforts to construct artificial supramolecular protein assemblies. However, despite their sophisticated structures, designed protein assemblies have yet to be incorporated into macroscale devices for real-life applications. We report a 2D crystalline protein assembly of C98/E57/E66 L-rhamnulose-1-phosphate aldolase ( CEE RhuA) that selectively blocks or passes molecular species when exposed to a chemical trigger. CEE RhuA crystals are engineered via cobalt(II) coordination bonds to undergo a coherent conformational change from a closed state (pore dimensions <1 nm) to an ajar state (pore dimensions ~4 nm) when exposed to an HCN(g) trigger. When layered onto a mesoporous silicon (pSi) photonic crystal optical sensor configured to detect HCN (g) , the 2D CEE RhuA crystal layer effectively blocks interferents that would otherwise result in a false positive signal. The 2D CEE RhuA crystal layer opens in selective response to low-ppm levels of HCN (g) , allowing analyte penetration into the pSi sensor layer for detection. These findings illustrate that designed protein assemblies can function as dynamic components of solid-state devices in non-aqueous environments.

Protein crystallization

Crystal (programming language)

10.1038/s41467-024-50567-8

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Citations (0)

Molecular lock regulates binding of glycine to a primitive NMDA receptor

Proceedings of the National Academy of Sciences (2016)

Alvin Yu Robert G. Alberstein Alecia Thomas Austin Zimmet Richard Grey

Significance Glycine-activated ionotropic glutamate receptors (iGluRs) encoded in ctenophore genomes are evolutionary precursors to NMDA receptors, which play important roles in synaptic plasticity. Ctenophore iGluRs feature a distinct interdomain salt bridge in the ligand-binding domain, a molecular lock, that thus far has not been found in iGluRs of other organisms. We use a combination of crystallographic, biochemical, electrophysiological, and computational approaches to elucidate the role of this molecular lock in a ctenophore iGluR. We find that perturbations to the lock can tune receptor kinetics and thermodynamics over very broad ranges. We also find that the strategic location of the lock may be the basis for the ligand-binding domain's extraordinarily high affinity for glycine.

Ionotropic glutamate receptor

10.1073/pnas.1607010113

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Citations (34)

Observations of the birth of crystals

Nature (2018)

Robert G. Alberstein F. Akif Tezcan

Protein crystallization

Crystal (programming language)

10.1038/d41586-018-03801-5

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Citations (14)