Shape-Persistent Macrocycles: A Synthetic Strategy that Combines Easy and Site-Specific Decorations with Improved Cyclization Efficiency

Junji Sakamoto; A. Dieter Schlüter

doi:10.1002/ejoc.200700118

Corner-, edge-, and facet-controlled growth of nanocrystals

Science Advances ◽

10.1126/sciadv.abf1410 ◽

2021 ◽

Vol 7 (3) ◽

pp. eabf1410

Author(s):

Yuanwei Li ◽

Haixin Lin ◽

Wenjie Zhou ◽

Lin Sun ◽

Devleena Samanta ◽

...

Keyword(s):

Energy Barrier ◽

Chemical Potential ◽

Specific Growth ◽

Control Structure ◽

Structure Evolution ◽

General Strategy ◽

Site Specific ◽

Synthetic Strategy ◽

Poor Understanding ◽

Exposed Facets

The ability to precisely control nanocrystal (NC) shape and composition is useful in many fields, including catalysis and plasmonics. Seed-mediated strategies have proven effective for preparing a wide variety of structures, but a poor understanding of how to selectively grow corners, edges, and facets has limited the development of a general strategy to control structure evolution. Here, we report a universal synthetic strategy for directing the site-specific growth of anisotropic seeds to prepare a library of designer nanostructures. This strategy leverages nucleation energy barrier profiles and the chemical potential of the growth solution to control the site-specific growth of NCs into exotic shapes and compositions. This strategy can be used to not only control where growth occurs on anisotropic seeds but also control the exposed facets of the newly grown regions. NCs of many shapes are synthesized, including over 10 here-to-fore never reported NCs and, in principle, many others are possible.

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Non-specific peptide size effects in the recognition by site-specific T-cell clones. Demonstration with a T site of myoglobin

Biochemical Journal ◽

10.1042/bj2460307 ◽

1987 ◽

Vol 246 (2) ◽

pp. 307-312 ◽

Cited By ~ 19

Author(s):

M Z Atassi ◽

M Yoshioka ◽

M Bean ◽

G S Bixler

Keyword(s):

T Cell ◽

Surface Region ◽

Protein Chain ◽

Uniform Size ◽

Site Specific ◽

T Cell Clones ◽

Synthetic Strategy ◽

Cell Clones ◽

Discrete Surface ◽

Lymph Node Cells

Six regions (T sites) of myoglobin (Mb) were found by a comprehensive synthetic strategy to stimulate Mb-primed lymph-node cells. To define precisely the N-terminal boundary of the immunodominant T site (residues 107-120) with site-specific T-cell clones and to determine the effects of peptide size on their stimulation, two sets of peptides were employed. In one set, the peptides were elongated to the left from His-113 by one-residue increments of the Mb sequence. The other set represented an identical stepwise elongation by one-residue increments of the Mb sequence, but which were extended by additional unrelated (‘nonsense’) residues to a uniform size of 14 residues. Examination of the proliferative responses of eight T-cell clones, derived from Mb-primed DBA/2 (H-2d) or SJL (H-2s) mice, revealed a dramatic non-specific size requirement. In every clone, the longer nonsense-extended peptides achieved maximum stimulating activity at a lower optimum peptide dose than its natural-sequence, but shorter, analogue. In addition, slight (one-residue) differences in the N-terminal boundaries among the clones was observed. Thus, the fine specificity of each clone was mapped to the region from residue 111 or 112 to about residue 120 of Mb, which coincides with the site of B-cell recognition and resides in a small discrete surface region of the protein chain.

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Large-cluster and combined fluorescent and gold immunoprobes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100166920 ◽

1996 ◽

Vol 54 ◽

pp. 892-893

Author(s):

Richard D. Powell ◽

James F. Hainfeld ◽

Carol M. R. Halsey ◽

David L. Spector ◽

Shelley Kaurin ◽

...

Keyword(s):

Metal Cluster ◽

Sulfonyl Chloride ◽

Gel Filtration ◽

Cross Linking ◽

Site Specific ◽

Fab Fragments ◽

Cluster Label ◽

Covalently Linked ◽

Texas Red ◽

Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

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The challenge of detecting modifications on proteins

Essays in Biochemistry ◽

10.1042/ebc20190055 ◽

2020 ◽

Vol 64 (1) ◽

pp. 135-153 ◽

Cited By ~ 1

Author(s):

Lauren Elizabeth Smith ◽

Adelina Rogowska-Wrzesinska

Keyword(s):

Mass Spectrometry ◽

Protein Function ◽

Chemical Properties ◽

Lysine Acetylation ◽

Mass Determination ◽

Post Translational Modifications ◽

Site Specific ◽

The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

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