On the prediction of crystal morphology. III. Equilibrium and growth behaviour of crystal faces containing multiple connected nets

Grimbergen, R. F. P.; Bennema, P.; Meekes, Hugo

doi:10.1107/s0108767398008897

Cited by 40 publications

(30 citation statements)

References 21 publications

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“…Thus, current data obtained for ␤2-m as well as the results discussed for Sup35 and A␤ peptide suggest that heterogeneity of structure is a common characteristic of amyloid fibrils. This could be partly consistent with the idea that the rate of crystal growth may be affected by bonding topology at the crystal surface (23).…”

Section: Direct Observation Of Amyloid Fibril Growth 16464supporting

confidence: 86%

Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence

Ban

Hamada

Hara

et al. 2003

Journal of Biological Chemistry

336

308

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Real-time monitoring of fibril growth is essential to clarify the mechanism of amyloid fibril formation. Thioflavin T (ThT) is a reagent known to become strongly fluorescent upon binding to amyloid fibrils. Here, we show that, by monitoring ThT fluorescence with total internal reflection fluorescence microscopy (TIRFM), amyloid fibrils of ␤2-microgobulin (␤2-m) can be visualized without requiring covalent fluorescence labeling. One of the advantages of TIRFM would be that we selectively monitor fibrils lying along the slide glass, so that we can obtain the exact length of fibrils. This method was used to follow the kinetics of seed-dependent ␤2-m fibril extension. The extension was unidirectional with various rates, suggesting the heterogeneity of the amyloid structures. Since ThT binding is common to all amyloid fibrils, the present method will have general applicability for the analysis of amyloid fibrils. We confirmed this with the octapeptide corresponding to the C terminus derived from human medin and the Alzheimer's amyloid ␤-peptide.There is an increasing body of evidence showing that many proteins including the Alzheimer's amyloid ␤-peptide (A␤), 1 prion protein, transthyretin, and ␤2-microgobulin (␤2-m) tend to misfold and aggregate into amyloid fibrils (1-3). Moreover, several proteins not known to be involved in disease and various polyamino acids have been shown to form amyloid fibrils in vitro under carefully selected conditions (4, 5). Although no sequence or structural similarity between the amyloid precursor proteins has been found, amyloid fibrils share several common structural and spectroscopic properties (6). Irrespective of the protein species, electron microscopy and x-ray fiber diffraction indicate that the amyloid fibrils have relatively rigid structures with diameters of 10 -15 nm consisting of cross-␤-strands. Making use of an NMR technique in combination with hydrogen/deuterium exchange of amide protons and dissolution of amyloid fibrils by dimethyl sulfoxide, we have shown that the amyloid fibrils of ␤2-m are stabilized by a hydrogenbond network which is more extensive than that in the native state (7).Amyloid fibril formation is considered to be a nucleation-dependent process in which non-native precursor proteins slowly associate to form the nuclei (8). This process is followed by an extension reaction, where the nucleus grows by sequential incorporation of more precursor protein molecules. This model has been validated by the observation that fibril extension kinetics is accelerated by the addition of preformed fibrils, i.e. by a seeding effect. However, the mechanism of fibril formation by individual polypeptide chains is not completely understood, and there are several variations of the nucleation-dependent model (9, 10). To address the mechanism of amyloid fibril formation, it is important to observe the process at the singlefibril level. Recently, epifluorescence with a newly introduced fluorescent dye (11) and atomic force microscopy (AFM) (12, 13) have been utilized for the d...

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Section: Direct Observation Of Amyloid Fibril Growth 16464supporting

confidence: 86%

Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence

Ban

Hamada

Hara

et al. 2003

Journal of Biological Chemistry

336

308

View full text Add to dashboard Cite

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“…It is usually impossible or impractical to use single crystal X-ray diffraction. To find the possible polymorph in which a given molecule can crystallize the researcher often needs to piece together experimental results such as the powder diffraction patterns and lattice energy calculations [3]. Polymorphism can cause profound problems in the development and formulation of organic and inorganic crystalline products.…”

Section: Introductionmentioning

confidence: 99%

Study of Polymorph Prediction For L-Ascorbic Acid

Arslantaş

Ermler

Yazici

et al. 2005

IJMS

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Possible polymorphs of L-ascorbic acid were investigated, considering eight space groups and assuming one molecule in the asymmetric unit. The grid-search method was compared with a Monte Carlo approach as performed in the Biosym / MSI polymorph Predictor. A number of possible crystal structures were found, including the experimental structure. Energy minimizations were performed with a united-atom force field. In all cases, the experimental structure had a low lattice energy. The number of hypothetical crystal structures was reduced considerably by removing space-group symmetry constraints, or by a primitive molecular dynamic shake-up. Nevertheless, sufficient structures of equal or lower energy compared with the experimental structure remained to suggest that other factors need to be considered for polymorph predictions of materials.

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“…The graph of Fig. 1 was introduced by Grimbergen et al [18] in their paper as type III. In the remainder of this paper we will refer to this structure as ''nonKossel''.…”

Section: Structurementioning

confidence: 99%

“…et al[18], since we do not use their strict solid-on-solid condition. The present graphs show that the growth rate of the {1 0 0} surfaces is hardly influenced by d, the growth rate of the {0 1 1} faces decreases for increasing d and the {0 0 1} faces turn from the slowest growing faces at low values of d into The bond strength / a is for all cases equal to 2kT.…”

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confidence: 99%